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- PDB-2yrc: Solution structure of the zf-Sec23_Sec24 from human Sec23A -

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Basic information

Entry
Database: PDB / ID: 2yrc
TitleSolution structure of the zf-Sec23_Sec24 from human Sec23A
ComponentsProtein transport protein Sec23AProtein targeting
KeywordsPROTEIN TRANSPORT / zinc binding / COPII / coat protein complex-II / endoplasmic reticulum / Golgi / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


COPII-coated vesicle cargo loading / COPII vesicle coat / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / COPII-mediated vesicle transport / extrinsic component of membrane / endoplasmic reticulum exit site / MHC class II antigen presentation / GTPase activator activity / protein localization to plasma membrane ...COPII-coated vesicle cargo loading / COPII vesicle coat / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / COPII-mediated vesicle transport / extrinsic component of membrane / endoplasmic reticulum exit site / MHC class II antigen presentation / GTPase activator activity / protein localization to plasma membrane / intracellular protein transport / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER to Golgi transport vesicle membrane / Golgi membrane / endoplasmic reticulum membrane / perinuclear region of cytoplasm / zinc ion binding / cytosol
Similarity search - Function
Sec23, C-terminal / Protein transport protein Sec23 / Sec23/Sec24, helical domain / Sec23/Sec24 beta-sandwich / Zinc finger, Sec23/Sec24-type superfamily / Sec23/Sec24 helical domain superfamily / Sec23/Sec24, trunk domain / Sec23/Sec24 zinc finger / Sec23/Sec24 trunk domain / Sec23/Sec24 helical domain ...Sec23, C-terminal / Protein transport protein Sec23 / Sec23/Sec24, helical domain / Sec23/Sec24 beta-sandwich / Zinc finger, Sec23/Sec24-type superfamily / Sec23/Sec24 helical domain superfamily / Sec23/Sec24, trunk domain / Sec23/Sec24 zinc finger / Sec23/Sec24 trunk domain / Sec23/Sec24 helical domain / Sec23/Sec24 beta-sandwich domain / Zn-finger domain of Sec23/24 / Zinc finger, Sec23/Sec24-type / Gelsolin-like domain superfamily / Gelsolin repeat / Gelsolin-like domain / ADF-H/Gelsolin-like domain superfamily / von Willebrand factor A-like domain superfamily / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Protein transport protein Sec23A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsNagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be Published
Title: Solution structure of the zf-Sec23_Sec24 from human Sec23A
Authors: Nagashima, T. / Hayashi, F. / Yokoyama, S.
History
DepositionApr 2, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 2, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein transport protein Sec23A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)6,5272
Polymers6,4611
Non-polymers651
Water0
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the least restraint violations, target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Protein transport protein Sec23A / Protein targeting / SEC23-related protein A


Mass: 6461.266 Da / Num. of mol.: 1 / Fragment: zf-Sec23_Sec24
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Plasmid: P060613-07 / References: UniProt: Q15436
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

DetailsContents: 1.12mM uniformly 13C, 15N-labeled protein; 20mM TrisHCl, 100mM NaCl, 1mM DTT, 0.02%NaN3, 0.05mM ZnCl2, 1mM IDA, 10% D2O, 90% H2O
Solvent system: 10% D2O / 90% H2O
Sample conditionsIonic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1CVariancollection
NMRPipe20020425Delaglio, F.processing
NMRView5.0.4Johnson, B.A.data analysis
Kujira0.9822Kobayashi, N.data analysis
CYANA2.0.17Guntert, P.structure solution
CYANA2.0.17Guntert, P.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations, target function
Conformers calculated total number: 100 / Conformers submitted total number: 20

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