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PDBsum entry 2w2j

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protein ligands metals links
Lyase PDB id
2w2j
Jmol
Contents
Protein chain
268 a.a. *
Ligands
GOL ×6
UNX ×3
Metals
_CL ×3
Waters ×336
* Residue conservation analysis
PDB id:
2w2j
Name: Lyase
Title: Crystal structure of the human carbonic anhydrase related protein viii
Structure: Carbonic anhydrase-related protein. Chain: a. Synonym: carp, carbonic anhydrase viii, ca-viii, ca8a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.60Å     R-factor:   0.201     R-free:   0.229
Authors: A.Kramm,J.R.C.Muniz,S.S.Picaud,F.Von Delft,E.S.Pilka,W.W.Yue O.N.F.King,G.Kochan,A.C.W.Pike,P.Filippakopoulos, C.Arrowsmith,M.Wikstrom,A.Edwards,C.Bountra,U.Oppermann
Key ref:
S.S.Picaud et al. (2009). Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing. Proteins, 76, 507-511. PubMed id: 19360879 DOI: 10.1002/prot.22411
Date:
31-Oct-08     Release date:   03-Feb-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P35219  (CAH8_HUMAN) -  Carbonic anhydrase-related protein
Seq:
Struc:
290 a.a.
268 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     one-carbon metabolic process   2 terms 
  Biochemical function     metal ion binding     3 terms  

 

 
DOI no: 10.1002/prot.22411 Proteins 76:507-511 (2009)
PubMed id: 19360879  
 
 
Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing.
S.S.Picaud, J.R.Muniz, A.Kramm, E.S.Pilka, G.Kochan, U.Oppermann, W.W.Yue.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Crystal structure of hCA VIII. (A) Ribbon diagram showing the secondary structure elements: -helices (red) and -strands (yellow). (B) C^ -superposition of hCA VIII (blue) and hCA XIII structures (cyan, PDB code 3DA2). The two loop regions that are unique in hCA VIII are shown in thick ribbons.
Figure 2.
Figure 2. Structural comparison of hCA VIII with the catalytic isozymes. (A) A close-up view showing the entrance of the hCA VIII cavity. hCA VIII is represented in blue ribbon, overlayed with a surface representation. (B) Active site of the CO[2]-bound hCA II (left, PDB code 3D92) and hCA VIII (right) structures. The hydrophobic CO[2] pocket is shown in pink surface. Spheres represent the Zn^2+ ion (black), water (red) and Cl^- ion (green). In the right panel, the CO[2] substrate from the hCA II structure (shown in dots) is superimposed onto the hCA VIII structure to illustrate the potential steric clash caused by I165 and I143 (green surface). (C) Schematic representation of the Zn^2+ coordination in hCA II (left), and Cl^- coordination in hCA VIII (right). Bond lengths are indicated in Å.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 76, 507-511) copyright 2009.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20356370 A.Aspatwar, M.E.Tolvanen, and S.Parkkila (2010).
Phylogeny and expression of carbonic anhydrase-related proteins.
  BMC Mol Biol, 11, 25.  
20219402 D.S.Froese, S.Healy, M.McDonald, G.Kochan, U.Oppermann, F.H.Niesen, and R.A.Gravel (2010).
Thermolability of mutant MMACHC protein in the vitamin B12-responsive cblC disorder.
  Mol Genet Metab, 100, 29-36.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.