2qxw
From Proteopedia
| Line 2: | Line 2: | ||
caption="2qxw, resolution 0.80Å" /> | caption="2qxw, resolution 0.80Å" /> | ||
'''Perdeuterated alr2 in complex with idd594'''<br /> | '''Perdeuterated alr2 in complex with idd594'''<br /> | ||
| + | |||
| + | ==Overview== | ||
| + | We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 A, 100K; 0.80 A, 15K; 1.75 A, 293K), neutron Laue data (2.2 A, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes. | ||
==About this Structure== | ==About this Structure== | ||
2QXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDP:'>NDP</scene>, <scene name='pdbligand=LDT:'>LDT</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] Known structural/functional Sites: <scene name='pdbsite=AC1:Ndp+Binding+Site+For+Residue+A+318'>AC1</scene>, <scene name='pdbsite=AC2:Ldt+Binding+Site+For+Residue+A+320'>AC2</scene>, <scene name='pdbsite=AC3:Cit+Binding+Site+For+Residue+A+400'>AC3</scene> and <scene name='pdbsite=AC4:Cit+Binding+Site+For+Residue+A+450'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QXW OCA]. | 2QXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDP:'>NDP</scene>, <scene name='pdbligand=LDT:'>LDT</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] Known structural/functional Sites: <scene name='pdbsite=AC1:Ndp+Binding+Site+For+Residue+A+318'>AC1</scene>, <scene name='pdbsite=AC2:Ldt+Binding+Site+For+Residue+A+320'>AC2</scene>, <scene name='pdbsite=AC3:Cit+Binding+Site+For+Residue+A+400'>AC3</scene> and <scene name='pdbsite=AC4:Cit+Binding+Site+For+Residue+A+450'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QXW OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase., Blakeley MP, Ruiz F, Cachau R, Hazemann I, Meilleur F, Mitschler A, Ginell S, Afonine P, Ventura ON, Cousido-Siah A, Haertlein M, Joachimiak A, Myles D, Podjarny A, Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1844-8. Epub 2008 Feb 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18250329 18250329] | ||
[[Category: Aldehyde reductase]] | [[Category: Aldehyde reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 32: | Line 38: | ||
[[Category: polymorphism]] | [[Category: polymorphism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:43:12 2008'' |
Revision as of 07:43, 14 March 2008
|
Perdeuterated alr2 in complex with idd594
Overview
We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 A, 100K; 0.80 A, 15K; 1.75 A, 293K), neutron Laue data (2.2 A, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes.
About this Structure
2QXW is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Aldehyde reductase, with EC number 1.1.1.21 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase., Blakeley MP, Ruiz F, Cachau R, Hazemann I, Meilleur F, Mitschler A, Ginell S, Afonine P, Ventura ON, Cousido-Siah A, Haertlein M, Joachimiak A, Myles D, Podjarny A, Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1844-8. Epub 2008 Feb 4. PMID:18250329
Page seeded by OCA on Fri Mar 14 09:43:12 2008
Categories: Aldehyde reductase | Homo sapiens | Single protein | Afonine, P. | Blakely, M. | Cachau, R. | Cousido-Siah, A. | Ginell, S. | Hazemann, I. | Joachimiak, A. | Meilleur, F. | Mitschler, A. | Myles, D. | Podjarny, A. | Ruiz, F. | Ventura, O. | CIT | LDT | NDP | Acetylation | Cataract | Cytoplasm | Idd594 | Nadp | Oxidoreductase | Polymorphism
