2qf7: Difference between revisions
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|PDB= 2qf7 |SIZE=350|CAPTION= <scene name='initialview01'>2qf7</scene>, resolution 2.000Å | |PDB= 2qf7 |SIZE=350|CAPTION= <scene name='initialview01'>2qf7</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SAP:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE+MONOTHIOPHOSPHATE'>SAP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] | ||
|GENE= pyc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29449 Rhizobium etli]) | |GENE= pyc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29449 Rhizobium etli]) | ||
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[[Category: multi-functional]] | [[Category: multi-functional]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:44:33 2008'' | ||
Revision as of 13:44, 23 March 2008
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| 2qf7, resolution 2.000Å | |||||||||||||
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| Ligands: | ZN, MG, CL, COA, SAP, GOL and FMT | ||||||||||||
| Gene: | pyc (Rhizobium etli) | ||||||||||||
| Activity: | Pyruvate carboxylase, with EC number 6.4.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of a complete multifunctional pyruvate carboxylase from Rhizobium etli
Overview
Biotin-dependent multifunctional enzymes carry out metabolically important carboxyl group transfer reactions and are potential targets for the treatment of obesity and type 2 diabetes. These enzymes use a tethered biotin cofactor to carry an activated carboxyl group between distantly spaced active sites. The mechanism of this transfer has remained poorly understood. Here we report the complete structure of pyruvate carboxylase at 2.0 angstroms resolution, which shows its domain arrangement. The structure, when combined with mutagenic analysis, shows that intermediate transfer occurs between active sites on separate polypeptide chains. In addition, domain rearrangements associated with activator binding decrease the distance between active-site pairs, providing a mechanism for allosteric activation. This description provides insight into the function of biotin-dependent enzymes and presents a new paradigm for multifunctional enzyme catalysis.
About this Structure
2QF7 is a Single protein structure of sequence from Rhizobium etli. Full crystallographic information is available from OCA.
Reference
Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme., St Maurice M, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I, Science. 2007 Aug 24;317(5841):1076-9. PMID:17717183
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