1dik: Difference between revisions

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[[Image:1dik.gif|left|200px]]
{{Seed}}
[[Image:1dik.png|left|200px]]


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{{STRUCTURE_1dik|  PDB=1dik  |  SCENE=  }}  
{{STRUCTURE_1dik|  PDB=1dik  |  SCENE=  }}  


'''PYRUVATE PHOSPHATE DIKINASE'''
===PYRUVATE PHOSPHATE DIKINASE===




==Overview==
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The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine domain is flanked by the nucleotide and the phosphoenolpyruvate/pyruvate domains, with the two substrate binding sites approximately 45 angstroms apart. The modes of substrate binding have been deduced by analogy to D-Ala-D-Ala ligase and to pyruvate kinase. Coupling between the two remote active sites is facilitated by two conformational states of the phosphohistidine domain. While the crystal structure represents the state of interaction with the nucleotide, the second state is achieved by swiveling around two flexible peptide linkers. This dramatic conformational transition brings the phosphocarrier residue in close proximity to phosphoenolpyruvate/pyruvate. The swiveling-domain paradigm provides an effective mechanism for communication in complex multidomain/multiactive site proteins.
The line below this paragraph, {{ABSTRACT_PUBMED_8610096}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8610096 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8610096}}


==About this Structure==
==About this Structure==
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[[Category: Kinase]]
[[Category: Kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:53:01 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:06:56 2008''

Revision as of 20:06, 30 June 2008

File:1dik.png

Template:STRUCTURE 1dik

PYRUVATE PHOSPHATE DIKINASE

Template:ABSTRACT PUBMED 8610096

About this Structure

1DIK is a Single protein structure of sequence from Clostridium symbiosum. Full crystallographic information is available from OCA.

Reference

Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites., Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D, Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2652-7. PMID:8610096

Page seeded by OCA on Mon Jun 30 23:06:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA, Joel L. Sussman

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