1dik

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[[Image:1dik.gif|left|200px]]
[[Image:1dik.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dik |SIZE=350|CAPTION= <scene name='initialview01'>1dik</scene>, resolution 2.3&Aring;
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The line below this paragraph, containing "STRUCTURE_1dik", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate,_phosphate_dikinase Pyruvate, phosphate dikinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.1 2.7.9.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PPDK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum])
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-->
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|DOMAIN=
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{{STRUCTURE_1dik| PDB=1dik | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dik OCA], [http://www.ebi.ac.uk/pdbsum/1dik PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dik RCSB]</span>
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}}
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'''PYRUVATE PHOSPHATE DIKINASE'''
'''PYRUVATE PHOSPHATE DIKINASE'''
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[[Category: Chen, C C.H.]]
[[Category: Chen, C C.H.]]
[[Category: Herzberg, O.]]
[[Category: Herzberg, O.]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:53:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:15 2008''
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Revision as of 10:53, 2 May 2008

Image:1dik.gif

Template:STRUCTURE 1dik

PYRUVATE PHOSPHATE DIKINASE


Overview

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.

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 Fri May 2 13:53:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA, Joel L. Sussman

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