1vbg
From Proteopedia
(New page: 200px<br /><applet load="1vbg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vbg, resolution 2.30Å" /> '''Pyruvate Phosphate D...) |
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| - | [[Image:1vbg.gif|left|200px]]<br /><applet load="1vbg" size=" | + | [[Image:1vbg.gif|left|200px]]<br /><applet load="1vbg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vbg, resolution 2.30Å" /> | caption="1vbg, resolution 2.30Å" /> | ||
'''Pyruvate Phosphate Dikinase from Maize'''<br /> | '''Pyruvate Phosphate Dikinase from Maize'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pyruvate phosphate dikinase (PPDK) reversibly catalyzes the conversion of | + | 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== | ==About this Structure== | ||
| - | 1VBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with MG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1VBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nakanishi, T.]] | [[Category: Nakanishi, T.]] | ||
[[Category: Nakatsu, T.]] | [[Category: Nakatsu, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sakata, K.]] | [[Category: Sakata, K.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:29 2008'' |
Revision as of 13:33, 21 February 2008
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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 with and as ligands. Active as Pyruvate, phosphate dikinase, with EC number 2.7.9.1 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
Page seeded by OCA on Thu Feb 21 15:33:29 2008
Categories: Pyruvate, phosphate dikinase | Single protein | Zea mays | Kato, H. | Matsuoka, M. | Nakanishi, T. | Nakatsu, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakata, K. | MG | SO4 | Maize | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Transferase
