1FWQ

SOLUTION STRUCTURE OF HUMAN MSS4, A GUANINE NUCLEOTIDE EXCHANGE FACTOR FOR RAB PROTEINS


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface.

Yu, H.Schreiber, S.L.

(1995) Nature 376: 788-791

  • DOI: https://doi.org/10.1038/376788a0
  • Primary Citation of Related Structures:  
    1FWQ

  • PubMed Abstract: 

    Guanine-nucleotide-exchange factors (GEFs) promote the exchange of GDP for GTP in Ras GTPases, and thereby positively regulate their functions. Members of the Sec4/Ypt1/Rab branch of the Ras superfamily are essential for vesicular transport. A GEF for a subset of Rab proteins, termed mammalian suppressor of Sec4 (Mss4), has been identified. Here we use multidimensional NMR to determine the structure of human Mss4 (hMss4), which is the first tertiary structure established for a protein with GEF activity. Mss4 contains a central beta-sheet sandwiched between two small sheets. It also binds a Zn2+ ion through Cys 23, Cys 26, Cys 94 and Cys 97. The Rab-binding surface of hMss4 has subsequently been delineated using chemical-shift perturbation experiments and site-directed mutagenesis. The active site of hMss4 involves the Zn(2+)-binding region and a neighbouring loop.


  • Organizational Affiliation

    Howard Hughes Medical Institute, Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GUANINE NUCLEOTIDE EXCHANGE FACTOR123Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P47224 (Homo sapiens)
Explore P47224 
Go to UniProtKB:  P47224
PHAROS:  P47224
GTEx:  ENSG00000183155 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP47224
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-10-04
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-05-22
    Changes: Data collection