1vbg: Difference between revisions

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


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{{STRUCTURE_1vbg|  PDB=1vbg  |  SCENE=  }}  
{{STRUCTURE_1vbg|  PDB=1vbg  |  SCENE=  }}  


'''Pyruvate Phosphate Dikinase from Maize'''
===Pyruvate Phosphate Dikinase from Maize===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15667207}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15667207 15667207]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15667207 15667207]
Purification, crystallization and preliminary X-ray diffraction studies on pyruvate phosphate dikinase from maize., Nakanishi T, Ohki Y, Oda J, Matsuoka M, Sakata K, Kato H, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):193-4. Epub 2003, Dec 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14684927 14684927]
Primary structure of maize pyruvate, orthophosphate dikinase as deduced from cDNA sequence., Matsuoka M, Ozeki Y, Yamamoto N, Hirano H, Kano-Murakami Y, Tanaka Y, J Biol Chem. 1988 Aug 15;263(23):11080-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2841317 2841317]
[[Category: Pyruvate, phosphate dikinase]]
[[Category: Pyruvate, phosphate dikinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transferase]]
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