1ika: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1ika.gif|left|200px]]
{{Seed}}
[[Image:1ika.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ika|  PDB=1ika  |  SCENE=  }}  
{{STRUCTURE_1ika|  PDB=1ika  |  SCENE=  }}  


'''STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE'''
===STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE===




==Overview==
<!--
The structure of the isocitrate dehydrogenase (IDH) complex with bound alpha-ketoglutarate, Ca2+, and NADPH was solved at 2.7-A resolution. The alpha-ketoglutarate binds in the active site at the same position and orientation as isocitrate, with a difference between the two bound molecules of about 0.8 A. The Ca2+ metal is coordinated by alpha-ketoglutarate, three conserved aspartate residues, and a pair of water molecules. The largest motion in the active site relative to the isocitrate enzyme complex is observed for tyrosine 160, which originally forms a hydrogen bond to the labile carboxyl group of isocitrate and moves to form a new hydrogen bond to Asp 307 in the complex with alpha-ketoglutarate. This triggers a number of significant movements among several short loops and adjoining secondary structural elements in the enzyme, most of which participate in dimer stabilization and formation of the active-site cleft. These rearrangements are similar to the ligand-binding-induced movements observed in globins and insulin and serve as a model for an enzymatic mechanism which involves local shifts of secondary structural elements during turnover, rather than large-scale domain closures or loop transitions induced by substrate binding such as those observed in hexokinase or triosephosphate isomerase.
The line below this paragraph, {{ABSTRACT_PUBMED_8369301}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8369301 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8369301}}


==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Junior, D E.Koshland.]]
[[Category: Junior, D E.Koshland.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:05:43 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:22:07 2008''

Revision as of 10:22, 1 July 2008

File:1ika.png

Template:STRUCTURE 1ika

STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE

Template:ABSTRACT PUBMED 8369301

About this Structure

1IKA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate., Stoddard BL, Koshland DE Jr, Biochemistry. 1993 Sep 14;32(36):9317-22. PMID:8369301

Page seeded by OCA on Tue Jul 1 13:22:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ika&oldid=612280"