1kc7
From Proteopedia
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| - | [[Image:1kc7.jpg|left|200px]] | + | [[Image:1kc7.jpg|left|200px]] |
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| - | '''Pyruvate Phosphate Dikinase with Bound Mg-phosphonopyruvate''' | + | {{Structure |
| + | |PDB= 1kc7 |SIZE=350|CAPTION= <scene name='initialview01'>1kc7</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PPR:PHOSPHONOPYRUVATE'>PPR</scene> | ||
| + | |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] | ||
| + | |GENE= PPDK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum]) | ||
| + | }} | ||
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| + | '''Pyruvate Phosphate Dikinase with Bound Mg-phosphonopyruvate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KC7 is a [ | + | 1KC7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC7 OCA]. |
==Reference== | ==Reference== | ||
| - | Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis., Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D, Biochemistry. 2002 Jan 22;41(3):780-7. PMID:[http:// | + | Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis., Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D, Biochemistry. 2002 Jan 22;41(3):780-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11790099 11790099] |
[[Category: Clostridium symbiosum]] | [[Category: Clostridium symbiosum]] | ||
[[Category: Pyruvate, phosphate dikinase]] | [[Category: Pyruvate, phosphate dikinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:15:25 2008'' |
Revision as of 10:15, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | PPDK (Clostridium symbiosum) | ||||||
| Activity: | Pyruvate, phosphate dikinase, with EC number 2.7.9.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Pyruvate Phosphate Dikinase with Bound Mg-phosphonopyruvate
Overview
Crystals of pyruvate phosphate dikinase in complex with a substrate analogue inhibitor, phosphonopyruvate (K(i) = 3 microM), have been obtained in the presence of Mg(2+). The structure has been determined and refined at 2.2 A resolution, revealing that the Mg(2+)-bound phosphonopyruvate binds in the alpha/beta-barrel's central channel, at the C-termini of the beta-strands. The mode of binding resembles closely the previously proposed PEP substrate binding mode, inferred by the homology of the structure (but not sequence homology) to pyruvate kinase. Kinetic analysis of site-directed mutants, probing residues involved in inhibitor binding, showed that all mutations resulted in inactivation, confirming the key role that these residues play in catalysis. Comparison between the structure of the PPDK-phosphonopyruvate complex and the structures of two complexes of pyruvate kinase, one with Mg(2+)-bound phospholactate and the other with Mg(2+)-oxalate and ATP, revealed that the two enzymes share some key features that facilitate common modes of substrate binding. There are also important structural differences; most notably, the machinery for acid/base catalysis is different.
About this Structure
1KC7 is a Single protein structure of sequence from Clostridium symbiosum. Full crystallographic information is available from OCA.
Reference
Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis., Herzberg O, Chen CC, Liu S, Tempczyk A, Howard A, Wei M, Ye D, Dunaway-Mariano D, Biochemistry. 2002 Jan 22;41(3):780-7. PMID:11790099
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