1h9b: 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:1h9b.jpg|left|200px]]
{{Seed}}
[[Image:1h9b.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h9b|  PDB=1h9b  |  SCENE=  }}  
{{STRUCTURE_1h9b|  PDB=1h9b  |  SCENE=  }}  


'''ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES'''
===ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES===




==Overview==
<!--
The reduced coenzymes NADH and NADPH only differ by one phosphate, but in the cell NADH provides reducing power for catabolism while NADPH is utilized in biosynthetic pathways. Enzymes almost invariably discriminate between the coenzymes, but glucose 6-phosphate dehydrogenase (G6PD) from Leuconostoc mesenteroides is rare in being functionally dual specific. In order to elucidate the coenzyme selectivity, the structures of NADP(+)- and NAD(+)-complexed L. mesenteroides G6PD have been determined including data to 2.2 and 2.5 A resolution, respectively, and compared with unliganded G6PD crystallized in the same space groups. Coenzyme binding is also compared with that in a ternary complex of a mutant in which Asp177 in the active site has been mutated to asparagine. There are no gross structural differences between the complexes. In both binary complexes, the enzyme interdomain hinge angle has opened. NADP(+) binds to the furthest open form; of the residues within the coenzyme domain, only Arg46 moves, interacting with the 2'-phosphate and adenine. NAD(+) is less well defined in the binding site; smaller hinge opening is seen but larger local changes: Arg46 is displaced, Thr14 bonds the 3'-hydroxyl and Gln47 bonds the 2'-hydroxyl. In the ternary complex, the hinge angle has closed; only the adenine nucleotide is ordered in the binding site. Arg46 again provides most binding interactions.
The line below this paragraph, {{ABSTRACT_PUBMED_11320304}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11320304 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11320304}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Naylor, C E.]]
[[Category: Naylor, C E.]]
[[Category: Glucose metabolism]]
[[Category: Glucose metabolism]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:35:55 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:47:28 2008''

Revision as of 04:48, 1 July 2008

File:1h9b.png

Template:STRUCTURE 1h9b

ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES

Template:ABSTRACT PUBMED 11320304

About this Structure

1H9B is a Single protein structure of sequence from Leuconostoc mesenteroides. Full crystallographic information is available from OCA.

Reference

NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:11320304

Page seeded by OCA on Tue Jul 1 07:47:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1h9b&oldid=606063"