PDBsum entry 1u8z

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protein ligands metals Protein-protein interface(s) links
Signaling protein PDB id
Protein chains
165 a.a. *
GDP ×2
_MG ×2
Waters ×505
* Residue conservation analysis
PDB id:
Name: Signaling protein
Title: Crystal structures of ral-gppnhp and ral-gdp reveal two novel binding sites that are also present in ras and rap
Structure: Ras-related protein ral-a. Chain: a, b. Engineered: yes
Source: Saguinus oedipus. Cotton-top tamarin. Organism_taxid: 9490. Gene: rala, ral-a, ral. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.50Å     R-factor:   0.202     R-free:   0.218
Authors: N.I.Nicely,J.Kosak,V.De Serrano,C.Mattos
Key ref:
N.I.Nicely et al. (2004). Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap. Structure, 12, 2025-2036. PubMed id: 15530367 DOI: 10.1016/j.str.2004.08.011
09-Aug-04     Release date:   23-Nov-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P63320  (RALA_SAGOE) -  Ras-related protein Ral-A
206 a.a.
165 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   3 terms 
  Biological process     signal transduction   5 terms 
  Biochemical function     GTP binding     2 terms  


DOI no: 10.1016/j.str.2004.08.011 Structure 12:2025-2036 (2004)
PubMed id: 15530367  
Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap.
N.I.Nicely, J.Kosak, Serrano, C.Mattos.
RalA is a GTPase with effectors such as Sec5 and Exo84 in the exocyst complex and RalBP1, a GAP for Rho proteins. We report the crystal structures of Ral-GppNHp and Ral-GDP. Disordered switch I and switch II, located away from crystal contacts, are observed in one of the molecules in the asymmetric unit of the Ral-GppNHp structure. In the other molecule in the asymmetric unit, a second Mg(2+) ion is bound to the GppNHp gamma-phosphate in an environment in which switch I is pulled away from the nucleotide and switch II is found in a tight beta turn. Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction. One site is adjacent to switch I. The other is modulated by switch II and is obstructed in Ral-GDP. The Ral structures are discussed in the context of the published structures of the Ral/Sec5 complex, Ras, and Rap.
  Selected figure(s)  
Figure 2.
Figure 2. The Asymmetric Unit in the Crystal Structure of Ral-GppNHPGppNHp is in cyan, Mg2+ is in yellow, and the coordinating water molecules are in red.
  The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 2025-2036) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20973973 B.U.Klink, and A.J.Scheidig (2010).
New insight into the dynamic properties and the active site architecture of H-Ras p21 revealed by X-ray crystallography at very high resolution.
  BMC Struct Biol, 10, 38.  
20696399 R.B.Fenwick, L.J.Campbell, K.Rajasekar, S.Prasannan, D.Nietlispach, J.Camonis, D.Owen, and H.R.Mott (2010).
The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction.
  Structure, 18, 985-995.
PDB codes: 2kwh 2kwi
18354782 L.E.Goldfinger (2008).
Choose your own path: specificity in Ras GTPase signaling.
  Mol Biosyst, 4, 293-299.  
17146673 M.Vogelsgesang, A.Pautsch, and K.Aktories (2007).
C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins.
  Naunyn Schmiedebergs Arch Pharmacol, 374, 347-360.  
16866878 A.Yanuar, S.Sakurai, K.Kitano, and T.Hakoshima (2006).
Crystal structure of human Rad GTPase of the RGK-family.
  Genes Cells, 11, 961-968.
PDB code: 2dpx
15920473 R.Jin, J.R.Junutula, H.T.Matern, K.E.Ervin, R.H.Scheller, and A.T.Brunger (2005).
Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase.
  EMBO J, 24, 2064-2074.
PDB codes: 1zc3 1zc4
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