1vbg

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|PDB= 1vbg |SIZE=350|CAPTION= <scene name='initialview01'>1vbg</scene>, resolution 2.30&Aring;
|PDB= 1vbg |SIZE=350|CAPTION= <scene name='initialview01'>1vbg</scene>, resolution 2.30&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [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]
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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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1vbh|1VBH]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vbg OCA], [http://www.ebi.ac.uk/pdbsum/1vbg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vbg RCSB]</span>
}}
}}
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Sakata, K.]]
[[Category: Sakata, K.]]
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[[Category: MG]]
 
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[[Category: SO4]]
 
[[Category: maize]]
[[Category: maize]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:43:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:22:00 2008''

Revision as of 21:22, 30 March 2008


PDB ID 1vbg

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: ,
Activity: Pyruvate, phosphate dikinase, with EC number 2.7.9.1
Related: 1VBH


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Pyruvate Phosphate Dikinase from Maize


Overview

Pyruvate phosphate dikinase (PPDK) reversibly catalyzes the conversion of ATP, phosphate, and pyruvate into AMP, pyrophosphate, and phosphoenolpyruvate (PEP), respectively. Since the nucleotide binding site (in the N-terminal domain) and the pyruvate/PEP binding site (in the C-terminal domain) are separated by approximately 45 A, it has been proposed that an intermediary domain, called the central domain, swivels between these remote domains to transfer the phosphate. However, no direct structural evidence for the swiveling central domain has been found. In this study, the crystal structures of maize PPDK with and without PEP have been determined at 2.3 A resolution. These structures revealed that the central domain is located near the pyruvate/PEP binding C-terminal domain, in contrast to the PPDK from Clostridium symbiosum, wherein the central domain is located near the nucleotide-binding N-terminal domain. Structural comparisons between the maize and C. symbiosum PPDKs demonstrated that the swiveling motion of the central domain consists of a rotation of at least 92 degrees and a translation of 0.5 A. By comparing the maize PPDK structures with and without PEP, we have elucidated the mode of binding of PEP to the C-terminal domain and the induced conformational changes in the central domain.

About this Structure

1VBG is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

Reference

Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion., Nakanishi T, Nakatsu T, Matsuoka M, Sakata K, Kato H, Biochemistry. 2005 Feb 1;44(4):1136-44. PMID:15667207

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