2qf7
From Proteopedia
(New page: 200px<br /><applet load="2qf7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qf7, resolution 2.000Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | Biotin-dependent multifunctional enzymes carry out metabolically important | + | 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== | ==About this Structure== | ||
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[[Category: Rhizobium etli]] | [[Category: Rhizobium etli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Maurice, M | + | [[Category: Maurice, M St.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Surinya, K | + | [[Category: Surinya, K H.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: COA]] | [[Category: COA]] | ||
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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 Thu Feb 21 18:38:49 2008'' |
Revision as of 16:38, 21 February 2008
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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 with , , , , , and as ligands. Active as Pyruvate carboxylase, with EC number 6.4.1.1 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
Page seeded by OCA on Thu Feb 21 18:38:49 2008
Categories: Pyruvate carboxylase | Rhizobium etli | Single protein | Maurice, M St. | Rayment, I. | Surinya, K H. | CL | COA | FMT | GOL | MG | SAP | ZN | Biotin-dependent | Ligase | Multi-domain | Multi-functional
