1pkm: Difference between revisions

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[[Image:1pkm.jpg|left|200px]]
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{{STRUCTURE_1pkm|  PDB=1pkm  |  SCENE=  }}  
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'''THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS'''
===THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS===




==Overview==
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The three-dimensional structure of cat-muscle pyoruvate kinase has been refined at a resolution of 2.6 A. The details of the structure permit interpretation of the original heavy-atom studies and give insight into the importance of conserved residues in pyruvate kinases and the allosteric behaviour of the enzyme. There are a small number of essential residues which determine the relative orientations of domains and the precise nature of intersubunit contacts. Arginine residues are particularly important.
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{{ABSTRACT_PUBMED_15299671}}


==About this Structure==
==About this Structure==
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[[Category: Muirhead, H.]]
[[Category: Muirhead, H.]]
[[Category: Pyruvate kinase]]
[[Category: Pyruvate kinase]]
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Revision as of 07:03, 28 July 2008

File:1pkm.png

Template:STRUCTURE 1pkm

THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS

Template:ABSTRACT PUBMED 15299671

About this Structure

1PKM is a Single protein structure of sequence from Felis catus. Full crystallographic information is available from OCA.

Reference

Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A., Allen SC, Muirhead H, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):499-504. PMID:15299671

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