1arl: Difference between revisions

Revision as of 17:28, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1arl.png

Template:STRUCTURE 1arl

CARBOXYPEPTIDASE A WITH ZN REMOVEDCARBOXYPEPTIDASE A WITH ZN REMOVED

Template:ABSTRACT PUBMED 9867434

About this StructureAbout this Structure

1ARL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Carboxypeptidase A: native, zinc-removed and mercury-replaced forms., Greenblatt HM, Feinberg H, Tucker PA, Shoham G, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):289-305. PMID:9867434

Page seeded by OCA on Mon Jun 30 17:28:28 2008

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OCA

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-[[Image:1arl.gif|left|200px]]
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 {{STRUCTURE_1arl|  PDB=1arl  |  SCENE=  }}
-'''CARBOXYPEPTIDASE A WITH ZN REMOVED'''
+===CARBOXYPEPTIDASE A WITH ZN REMOVED===
-==Overview==
+<!--
-The crystal structure of the zinc-containing exopeptidase bovine carboxypeptidase A (CPA) has been refined to high resolution, based on a data set collected from a single crystal, incorporating new sequence information based on cloning of the bovine gene. In addition, new refined structures are available for the zinc-removed form of the enzyme, apo-CPA, as well as the mercury-replaced form, Hg-CPA. The native structure reveals that the zinc-bound water molecule does not appear to more loosely bound than the rest of the zinc ligands, at least when B-factor values are considered. Nor is there any evidence for a secondary location of this water molecule. The apo-enzyme structure does not show any density in the place of the removed zinc ion. The only significant change appears to be a chi2 rotation of one zinc histidine ligand to form an ion-pair interaction with a glutamic acid side chain. The structure of Hg-CPA reveals a solvent Tris molecule bound to the mercury cation, as well as an unidentified cation bound to Glu270. The location of this citation agrees with previous proposals for the binding side of inhibitory zinc. These observations may explain some of the differences in kinetics observed in metal- replaced CPA.
+The line below this paragraph, {{ABSTRACT_PUBMED_9867434}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9867434 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9867434}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Metalloproteinase]]
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