1ka2

From Proteopedia

(Difference between revisions)

Revision as of 21:34, 9 September 2015

Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg

Structural highlights

1ka2 is a 1 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1k9x, 1ka4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CBP1_PYRFU] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.

Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.,Arndt JW, Hao B, Ramakrishnan V, Cheng T, Chan SI, Chan MK Structure. 2002 Feb;10(2):215-24. PMID:11839307^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cheng TC, Ramakrishnan V, Chan SI. Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. Protein Sci. 1999 Nov;8(11):2474-86. PMID:10595552 doi:http://dx.doi.org/10.1110/ps.8.11.2474
↑ Arndt JW, Hao B, Ramakrishnan V, Cheng T, Chan SI, Chan MK. Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. Structure. 2002 Feb;10(2):215-24. PMID:11839307

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ka2"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k9x|1k9x]], [[1ka4|1ka4]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ka2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ka2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ka2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ka2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka2 OCA], [http://pdbe.org/1ka2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ka2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ka2 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q8U3L0_PYRFU Q8U3L0_PYRFU]] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.<ref>PMID:10595552</ref>
+[[http://www.uniprot.org/uniprot/CBP1_PYRFU CBP1_PYRFU]] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.<ref>PMID:10595552</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ka2" style="background-color:#fffaf0;"></div>
 ==See Also==

1ka2

From Proteopedia

Revision as of 21:34, 9 September 2015

Structure of Pyrococcus furiosus Carboxypeptidase Apo-Mg

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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