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- EMDB-22630: Partial open state of Mycobacterium tuberculosis zinc metalloprot... -

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Open data


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Basic information

Entry
Database: EMDB / ID: EMD-22630
TitlePartial open state of Mycobacterium tuberculosis zinc metalloprotease 1
Map data
Sample
  • Complex: Mycobacterium tuberculosis zinc metalloprotease partial open state
    • Protein or peptide: Zinc metalloprotease
KeywordsOpen state / HYDROLASE
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases / protein processing / metalloendopeptidase activity / metal ion binding / plasma membrane
Similarity search - Function
Neprilysin-like (M13) protease domain profile. / Peptidase M13 / Peptidase M13, N-terminal domain / Peptidase M13, C-terminal domain / Peptidase M13, domain 2 / Peptidase family M13 / Peptidase family M13 / Metallopeptidase, catalytic domain superfamily
Similarity search - Domain/homology
Zinc metalloprotease / Probable zinc metalloprotease Zmp1
Similarity search - Component
Biological speciesMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.6 Å
AuthorsMancl JM / Liang WG
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)R01 GM121964 United States
CitationJournal: Structure / Year: 2021
Title: Structural analysis of Mycobacterium tuberculosis M13 metalloprotease Zmp1 open states.
Authors: Wenguang G Liang / Jordan M Mancl / Minglei Zhao / Wei-Jen Tang /
Abstract: Zinc metalloprotease 1 (Zmp1), a Mycobacterium tuberculosis 75 kDa secreted enzyme, mediates key stages of tuberculosis disease progression. The biological activity of Zmp1 presumably stems from its ...Zinc metalloprotease 1 (Zmp1), a Mycobacterium tuberculosis 75 kDa secreted enzyme, mediates key stages of tuberculosis disease progression. The biological activity of Zmp1 presumably stems from its ability to degrade bacterium- and/or host-derived peptides. The crystal structures of Zmp1 and related M13 metalloproteases, such as neprilysin and endothelin-converting enzyme-1 were determined only in the closed conformation, which cannot capture substrates or release proteolytic products. Thus, the mechanisms of substrate binding and selectivity remain elusive. Here we report two open-state cryo-EM structures of Zmp1, revealed by our SAXS analysis to be the dominant states in solution. Our structural analyses reveal how ligand binding induces a conformational switch in four linker regions to drive the rigid body motion of the D1 and D2 domains, which form the sizable catalytic chamber. Furthermore, they offer insights into the catalytic cycle and mechanism of substrate recognition of M13 metalloproteases for future therapeutic innovations.
History
DepositionSep 8, 2020-
Header (metadata) releaseDec 23, 2020-
Map releaseDec 23, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 5
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 5
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7k1v
  • Surface level: 5
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_22630.png

Downloads & links

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Map

FileDownload / File: emd_22630.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.063 Å
Density
Contour LevelBy AUTHOR: 5.0 / Movie #1: 5
Minimum - Maximum-17.952086999999999 - 29.145693000000001
Average (Standard dev.)-0.000000000000877 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions180180180
Spacing180180180
CellA=B=C: 191.34 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0631.0631.063
M x/y/z180180180
origin x/y/z0.0000.0000.000
length x/y/z191.340191.340191.340
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ180180180
MAP C/R/S321
start NC/NR/NS000
NC/NR/NS180180180
D min/max/mean-17.95229.146-0.000

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Supplemental data

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Sample components

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Entire : Mycobacterium tuberculosis zinc metalloprotease partial open state

EntireName: Mycobacterium tuberculosis zinc metalloprotease partial open state
Components
  • Complex: Mycobacterium tuberculosis zinc metalloprotease partial open state
    • Protein or peptide: Zinc metalloprotease

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Supramolecule #1: Mycobacterium tuberculosis zinc metalloprotease partial open state

SupramoleculeName: Mycobacterium tuberculosis zinc metalloprotease partial open state
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Strain: ATCC 25618 / H37Rv

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Macromolecule #1: Zinc metalloprotease

MacromoleculeName: Zinc metalloprotease / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Metalloendopeptidases
Source (natural)Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
Molecular weightTheoretical: 78.019797 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDHPFTMTLA IPSGIDLSHI DADARPQDDL FGHVNGRWLA EHEIPADRAT DGAFRSLFD RAETQVRDLI IQASQAGAAV GTDAQRIGDL YASFLDEEAV ERAGVQPLHD ELATIDSAAD ATELAAALGT L QRAGVGGG ...String:
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDHPFTMTLA IPSGIDLSHI DADARPQDDL FGHVNGRWLA EHEIPADRAT DGAFRSLFD RAETQVRDLI IQASQAGAAV GTDAQRIGDL YASFLDEEAV ERAGVQPLHD ELATIDSAAD ATELAAALGT L QRAGVGGG IGVYVDTDSK DSTRYLVHFT QSGIGLPDES YYRDEQHAAV LAAYPGHIAR MFGLVYGGES RDHAKTADRI VA LETKLAD AHWDVVKRRD ADLGYNLRTF AQLQTEGAGF DWVSWVTALG SAPDAMTELV VRQPDYLVTF ASLWASVNVE DWK CWARWR LIRARAPWLT RALVAEDFEF YGRTLTGAQQ LRDRWKRGVS LVENLMGDAV GKLYVQRHFP PDAKSRIDTL VDNL QEAYR ISISELDWMT PQTRQRALAK LNKFTAKVGY PIKWRDYSKL AIDRDDLYGN VQRGYAVNHD RELAKLFGPV DRDEW FMTP QTVNAYYNPG MNEIVFPAAI LQPPFFDPQA DEAANYGGIG AVIGHEIGHG FDDQGAKYDG DGNLVDWWTD DDRTEF AAR TKALIEQYHA YTPRDVDHPG PPHVQGAFTI GENIGDLGGL SIALLAYQLS LNGNPAPVID GLTGMQRVFF GWAQIWR TK SRAAEAIRRL AVDPHSPPEF RCNGVVRNVD AFYQAFDVTE DDALFLDPQR RVRIWN

UniProtKB: Zinc metalloprotease

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.8 mg/mL
BufferpH: 6.8
Details: 20 mM HEPES, pH 6.8, 150 mM NaCl, 0.5 mM BME, 20 mM Trimethylamine N-oxide dihydrate
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 308 K / Instrument: FEI VITROBOT MARK II

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average exposure time: 5.0 sec. / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.4000000000000001 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 8342000
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 441846
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final 3D classificationSoftware - Name: RELION (ver. 3.1)

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Atomic model buiding 1

Initial modelPDB ID:

6xly


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-7k1v:
Partial open state of Mycobacterium tuberculosis zinc metalloprotease 1

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