[English] 日本語
Yorodumi
- PDB-5cqc: Crystal structure of the legionella pneumophila effector protein RavZ -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5cqc
TitleCrystal structure of the legionella pneumophila effector protein RavZ
Componentsputative RavZ protein
KeywordsHYDROLASE / Ulp-family cysteine protease / autophagy inhibitor / PI3P binding domain / legionella pneumophila effector protein
Function / homology
Function and homology information


host intracellular membrane-bounded organelle / symbiont-mediated suppression of host autophagy / protein delipidation / phosphatidylinositol-3-phosphate binding / cysteine-type peptidase activity / host cell cytoplasmic vesicle membrane / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / proteolysis / extracellular region / membrane
Similarity search - Function
: / Cysteine protease RavZ
Similarity search - Component
Biological speciesLegionella pneumophila (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.985 Å
AuthorsHorenkamp, F.A. / Reinisch, K.M.
CitationJournal: Dev.Cell / Year: 2015
Title: The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs.
Authors: Horenkamp, F.A. / Kauffman, K.J. / Kohler, L.J. / Sherwood, R.K. / Krueger, K.P. / Shteyn, V. / Roy, C.R. / Melia, T.J. / Reinisch, K.M.
History
DepositionJul 21, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 9, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 23, 2015Group: Database references
Revision 1.2Sep 30, 2015Group: Database references
Revision 1.3Mar 6, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: putative RavZ protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,2562
Polymers47,1191
Non-polymers1371
Water181
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)221.778, 221.778, 72.536
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number97
Space group name H-MI422

-
Components

#1: Protein putative RavZ protein


Mass: 47118.910 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Legionella pneumophila (bacteria) / Gene: lpg1683 / Plasmid: pGex6P1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q5ZUV9
#2: Chemical ChemComp-BA / BARIUM ION


Mass: 137.327 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ba
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 4.73 Å3/Da / Density % sol: 74.01 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, hanging drop / pH: 5.1 / Details: 12% PEG 3350, 0.2 M BaCl2, 0.1 M MES

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 9, 2014
RadiationMonochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.98→110 Å / Num. all: 18551 / Num. obs: 18194 / % possible obs: 99.2 % / Redundancy: 5.7 % / Rmerge(I) obs: 0.066 / Net I/σ(I): 17.3
Reflection shellResolution: 2.98→3.14 Å / Redundancy: 5.9 % / Mean I/σ(I) obs: 0.9 / % possible all: 98.2

-
Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.985→68.942 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2504 1818 10 %random selection
Rwork0.2143 ---
obs0.218 18179 97.13 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.985→68.942 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2606 0 1 1 2608
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0092653
X-RAY DIFFRACTIONf_angle_d1.3293609
X-RAY DIFFRACTIONf_dihedral_angle_d14.432903
X-RAY DIFFRACTIONf_chiral_restr0.052428
X-RAY DIFFRACTIONf_plane_restr0.005460
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9849-3.06560.44841080.3916966X-RAY DIFFRACTION77
3.0656-3.15580.42661390.36821249X-RAY DIFFRACTION97
3.1558-3.25770.38571390.3091256X-RAY DIFFRACTION100
3.2577-3.37410.31421420.26411275X-RAY DIFFRACTION100
3.3741-3.50920.30751400.28781259X-RAY DIFFRACTION99
3.5092-3.66890.30241420.21641290X-RAY DIFFRACTION99
3.6689-3.86230.24691400.21981255X-RAY DIFFRACTION99
3.8623-4.10420.29041440.20421291X-RAY DIFFRACTION99
4.1042-4.42110.29311400.18921272X-RAY DIFFRACTION99
4.4211-4.86590.18641450.17031299X-RAY DIFFRACTION99
4.8659-5.56970.19851440.18681291X-RAY DIFFRACTION99
5.5697-7.01620.25391440.24491303X-RAY DIFFRACTION99
7.0162-68.96060.22671510.20151355X-RAY DIFFRACTION96
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.15320.35050.46884.6442.89618.1669-0.29440.04860.3533-0.31920.0667-0.0586-0.5721-0.18210.2860.6985-0.0739-0.0160.4480.08340.6864277.717187.22083.1378
22.521-3.5722-0.99877.4004-1.62364.86280.00180.49520.9204-0.3643-0.0905-0.8412-0.50090.78190.09460.9138-0.17830.03350.7620.0670.8192288.9077180.9791-6.3251
31.1550.2186-0.13951.82262.15085.54780.0697-0.12390.719-0.128-0.02560.113-1.76140.2896-0.11241.512-0.1154-0.05630.5664-0.08361.2897279.7884203.56822.7047
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 49 through 167 )
2X-RAY DIFFRACTION2chain 'A' and (resid 168 through 256 )
3X-RAY DIFFRACTION3chain 'A' and (resid 257 through 429 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more