1ai2
From Proteopedia
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[[Image:1ai2.gif|left|200px]] | [[Image:1ai2.gif|left|200px]] | ||
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- | | | + | {{STRUCTURE_1ai2| PDB=1ai2 | SCENE= }} |
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'''ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)''' | '''ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)''' | ||
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==About this Structure== | ==About this Structure== | ||
- | 1AI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry | + | 1AI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ikb 1ikb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AI2 OCA]. |
==Reference== | ==Reference== | ||
Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences., Mesecar AD, Stoddard BL, Koshland DE Jr, Science. 1997 Jul 11;277(5323):202-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9211842 9211842] | Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences., Mesecar AD, Stoddard BL, Koshland DE Jr, Science. 1997 Jul 11;277(5323):202-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9211842 9211842] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Junior, D E.Koshland.]] | [[Category: Junior, D E.Koshland.]] | ||
[[Category: Mesecar, A.]] | [[Category: Mesecar, A.]] | ||
[[Category: Stoddard, B L.]] | [[Category: Stoddard, B L.]] | ||
- | [[Category: | + | [[Category: Glyoxylate bypass]] |
- | [[Category: | + | [[Category: Nadp]] |
- | [[Category: | + | [[Category: Phosphorylation]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:17:48 2008'' | |
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:17, 2 May 2008
ISOCITRATE DEHYDROGENASE COMPLEXED WITH ISOCITRATE, NADP+, AND CALCIUM (FLASH-COOLED)
Overview
Small structural perturbations in the enzyme isocitrate dehydrogenase (IDH) were made in order to evaluate the contribution of precise substrate alignment to the catalytic power of an enzyme. The reaction trajectory of IDH was modified (i) after the adenine moiety of nicotinamide adenine dinucleotide phosphate was changed to hypoxanthine (the 6-amino was changed to 6-hydroxyl), and (ii) by replacing Mg2+, which has six coordinating ligands, with Ca2+, which has eight coordinating ligands. Both changes make large (10(-3) to 10(-5)) changes in the reaction velocity but only small changes in the orientation of the substrates (both distance and angle) as revealed by cryocrystallographic trapping of active IDH complexes. The results provide evidence that orbital overlap produced by optimal orientation of reacting orbitals plays a major quantitative role in the catalytic power of enzymes.
About this Structure
1AI2 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1ikb. Full crystallographic information is available from OCA.
Reference
Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences., Mesecar AD, Stoddard BL, Koshland DE Jr, Science. 1997 Jul 11;277(5323):202-6. PMID:9211842 Page seeded by OCA on Fri May 2 10:17:48 2008