3icd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:3icd.jpg|left|200px]]
[[Image:3icd.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 3icd |SIZE=350|CAPTION= <scene name='initialview01'>3icd</scene>, resolution 2.5&Aring;
+
The line below this paragraph, containing "STRUCTURE_3icd", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_3icd| PDB=3icd | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3icd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3icd OCA], [http://www.ebi.ac.uk/pdbsum/3icd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3icd RCSB]</span>
+
-
}}
+
'''STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE'''
'''STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE'''
Line 24: Line 21:
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase., Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM, Proc Natl Acad Sci U S A. 1989 Nov;86(22):8635-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2682654 2682654]
Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase., Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM, Proc Natl Acad Sci U S A. 1989 Nov;86(22):8635-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2682654 2682654]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Isocitrate dehydrogenase (NADP(+))]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Helmers, N H.]]
[[Category: Helmers, N H.]]
Line 32: Line 28:
[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
[[Category: Thorsness, P E.]]
[[Category: Thorsness, P E.]]
-
[[Category: oxidoreductase (nad(a)-choh(d))]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:04:40 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:34:04 2008''
+

Revision as of 19:04, 4 May 2008

Template:STRUCTURE 3icd

STRUCTURE OF A BACTERIAL ENZYME REGULATED BY PHOSPHORYLATION, ISOCITRATE DEHYDROGENASE


Overview

The structure of isocitrate dehydrogenase [threo-DS-isocitrate: NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42] from Escherichia coli has been solved and refined at 2.5 A resolution and is topologically different from that of any other dehydrogenase. This enzyme, a dimer of identical 416-residue subunits, is inactivated by phosphorylation at Ser-113, which lies at the edge of an interdomain pocket that also contains many residues conserved between isocitrate dehydrogenase and isopropylmalate dehydrogenase. Isocitrate dehydrogenase contains an unusual clasp-like domain in which both polypeptide chains in the dimer interlock. Based on the structure of isocitrate dehydrogenase and conservation with isopropylmalate dehydrogenase, we suggest that the active site lies in an interdomain pocket close to the phosphorylation site.

About this Structure

3ICD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase., Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE Jr, Stroud RM, Proc Natl Acad Sci U S A. 1989 Nov;86(22):8635-9. PMID:2682654 Page seeded by OCA on Sun May 4 22:04:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools