1ne7: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1ne7.gif|left|200px]]
{{Seed}}
[[Image:1ne7.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ne7|  PDB=1ne7  |  SCENE=  }}  
{{STRUCTURE_1ne7|  PDB=1ne7  |  SCENE=  }}  


'''HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE'''
===HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE===




==Overview==
<!--  
Glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D-glucosamine-6-phosphate into D-fructose-6-phosphate and ammonium. Here we describe the existence of two mammalian glucosamine-6-phosphate deaminase enzymes. We present the crystallographic structure of one of them, the long human glucosamine-6-phosphate deaminase, at 1.75 A resolution. Crystals belong to the space group P2(1)2(1)2(1) and present a whole hexamer in the asymmetric unit. The active-site lid (residues 162-182) presented significant structural differences among monomers. Interestingly the region with the largest differences, when compared with the Escherichia coli homologue, was found to be close to the active site. These structural differences can be related to the kinetic and allosteric properties of both mammalian enzymes.
The line below this paragraph, {{ABSTRACT_PUBMED_12965206}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12965206 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12965206}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Conformational disorder]]
[[Category: Conformational disorder]]
[[Category: V-type like allosteric enzyme]]
[[Category: V-type like allosteric enzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:25:34 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:08:19 2008''

Revision as of 16:08, 28 July 2008

File:1ne7.png

Template:STRUCTURE 1ne7

HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE

Template:ABSTRACT PUBMED 12965206

About this Structure

1NE7 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1d9t. Full crystallographic information is available from OCA.

Reference

Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study., Arreola R, Valderrama B, Morante ML, Horjales E, FEBS Lett. 2003 Sep 11;551(1-3):63-70. PMID:12965206

Page seeded by OCA on Mon Jul 28 19:08:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ne7&oldid=711442"