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PDBsum entry 2fna

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protein ligands metals Protein-protein interface(s) links
Atp-binding protein PDB id
2fna
Jmol
Contents
Protein chains
352 a.a. *
Ligands
ADP ×2
EDO ×7
Metals
_MG ×2
Waters ×348
* Residue conservation analysis
PDB id:
2fna
Name: Atp-binding protein
Title: Crystal structure of an archaeal aaa+ atpase (sso1545) from solfataricus p2 at 2.00 a resolution
Structure: Conserved hypothetical protein. Chain: a, b. Engineered: yes
Source: Sulfolobus solfataricus. Organism_taxid: 273057. Strain: p2. Gene: 13814777. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.177     R-free:   0.226
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
Q.Xu et al. (2009). Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus. Proteins, 74, 1041-1049. PubMed id: 19089981 DOI: 10.1002/prot.22325
Date:
10-Jan-06     Release date:   07-Feb-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 352 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleotide binding     2 terms  

 

 
DOI no: 10.1002/prot.22325 Proteins 74:1041-1049 (2009)
PubMed id: 19089981  
 
 
Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus.
Q.Xu, C.L.Rife, D.Carlton, M.D.Miller, S.S.Krishna, M.A.Elsliger, P.Abdubek, T.Astakhova, H.J.Chiu, T.Clayton, L.Duan, J.Feuerhelm, S.K.Grzechnik, J.Hale, G.W.Han, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, A.Kumar, D.McMullan, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, R.Reyes, H.van den Bedem, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 2.
Figure 2. Surface conservation pattern and the nucleotide binding site of SSO1545. A: Molecular surface of SSO1545 colored by sequence conservation. The most conserved residues are shown in red, the nonconserved residues in white. The three domains of SSO1543 are shown in ribbon representation and colored as yellow, blue, and cyan, respectively. The orientation of left panel is the same as in Figure 1(A). B: Close-up stereo view of the ADP binding site. The bound ADP (yellow) and magnesium ion (silver) are shown in sticks and sphere, respectively. Walker A (P-loop, green), Walker B (W-B, blue), sensor I (S-I, cyan), sensor II (S-II, white) are shown in cartoon and sticks. The STAND-specific hhGRExE and GxP motifs are also highlighted in blue.
Figure 3.
Figure 3. Structural comparisons of SSO1545 with AAA+ ATPases with similar domain organizations: Orc1 (PDB 2v1u), RuvB (PDB 1in5), Orc2 (PDB 1w5t), and Apaf-1 (PDB 1z6t, residues 105-450). These structures were superimposed base on their respective NTPase domains (gray). The linker regions connecting the NTPase domain and the WH domain (green) are shown in red. The nucleotides and magnesium ions are shown in sticks and spheres, respectively.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 74, 1041-1049) copyright 2009.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20693326 E.Marquenet, and E.Richet (2010).
Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli.
  J Bacteriol, 192, 5181-5191.  
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