1ekj: Difference between revisions

Revision as of 00:53, 1 July 2008

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File:1ekj.png

Template:STRUCTURE 1ekj

THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUMTHE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM

Template:ABSTRACT PUBMED 10747009

About this StructureAbout this Structure

1EKJ is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.

ReferenceReference

The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases., Kimber MS, Pai EF, EMBO J. 2000 Apr 3;19(7):1407-18. PMID:10747009

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OCA

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-[[Image:1ekj.gif|left|200px]]
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-'''THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM'''
+===THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM===
-==Overview==
+<!--
-We have determined the structure of the beta-carbonic anhydrase from the dicotyledonous plant Pisum sativum at 1.93 A resolution, using a combination of multiple anomalous scattering off the active site zinc ion and non-crystallographic symmetry averaging. The mol- ecule assembles as an octamer with a novel dimer of dimers of dimers arrangement. Two distinct patterns of conservation of active site residues are observed, implying two potentially mechanistically distinct classes of beta-carbonic anhydrases. The active site is located at the interface between two monomers, with Cys160, His220 and Cys223 binding the catalytic zinc ion and residues Asp162 (oriented by Arg164), Gly224, Gln151, Val184, Phe179 and Tyr205 interacting with the substrate analogue, acetic acid. The substrate binding groups have a one to one correspondence with the functional groups in the alpha-carbonic anhydrase active site, with the corresponding residues being closely superimposable by a mirror plane. Therefore, despite differing folds, alpha- and beta-carbonic anhydrase have converged upon a very similar active site design and are likely to share a common mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_10747009}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10747009 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10747009}}
 ==About this Structure==
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 [[Category: Rossman fold domain]]
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