1yba
From Proteopedia
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| - | [[Image:1yba.gif|left|200px]] | + | [[Image:1yba.gif|left|200px]] |
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| - | '''The active form of phosphoglycerate dehydrogenase''' | + | {{Structure |
| + | |PDB= 1yba |SIZE=350|CAPTION= <scene name='initialview01'>1yba</scene>, resolution 2.24Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoglycerate_dehydrogenase Phosphoglycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.95 1.1.1.95] | ||
| + | |GENE= serA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''The active form of phosphoglycerate dehydrogenase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YBA is a [ | + | 1YBA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBA OCA]. |
==Reference== | ==Reference== | ||
| - | Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase., Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ, Biochemistry. 2005 Apr 19;44(15):5763-73. PMID:[http:// | + | Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase., Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ, Biochemistry. 2005 Apr 19;44(15):5763-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15823035 15823035] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoglycerate dehydrogenase]] | [[Category: Phosphoglycerate dehydrogenase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 15:20:40 2008'' |
Revision as of 13:20, 20 March 2008
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| , resolution 2.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | serA (Escherichia coli) | ||||||
| Activity: | Phosphoglycerate dehydrogenase, with EC number 1.1.1.95 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The active form of phosphoglycerate dehydrogenase
Overview
An active conformation of phosphoglycerate dehydrogenase (PGDH) from Escherichia coli has been obtained using X-ray crystallography. The X-ray crystal structure is used to examine the potential intermediates for V(max) regulation, for the redox reaction, and for cooperative effects of serine binding. The crystal structure at 2.2 A resolution contains bound NAD(+) cofactor, either sulfate or phosphate anions, and alpha-ketoglutarate, a nonphysiological substrate. A PGDH subunit is formed from three distinct domains: regulatory (RBD), substrate (SBD), and nucleotide binding (NBD). The crystal conformation of the homotetramer points to the fact that, in the absence of serine, coordinated movement of the RBD-SBD domains occurs relative to the NBD. The result is a conformational change involving the steric relationships of both the domains and the subunits. Within the active site of each subunit is a bound molecule of alpha-ketoglutarate and the coenzyme, NAD. The catalytic or active site cleft is changed slightly although it is still solvent exposed; therefore, the catalytic reaction probably involves additional conformational changes. By comparing the inhibited with the uninhibited complex, it is possible to describe changes in conformation that are involved in the inhibitory signal transduction of serine.
About this Structure
1YBA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase., Thompson JR, Bell JK, Bratt J, Grant GA, Banaszak LJ, Biochemistry. 2005 Apr 19;44(15):5763-73. PMID:15823035
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