1cru: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1cru.gif|left|200px]] | [[Image:1cru.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1cru", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1cru| PDB=1cru | SCENE= }} | ||
}} | |||
'''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE''' | '''SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE''' | ||
| Line 29: | Line 26: | ||
[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
[[Category: | [[Category: Beta-propeller]] | ||
[[Category: | [[Category: Complex with the cofactor pqq and the inhibitor methylhydrazine]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Superbarrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:02:59 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 10:02, 2 May 2008
SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE
Overview
Soluble glucose dehydrogenase (s-GDH) from the bacterium Acinetobacter calcoaceticus is a classical quinoprotein. It requires the cofactor pyrroloquinoline quinone (PQQ) to catalyze the oxidation of glucose to gluconolactone. The precise catalytic role of PQQ in s-GDH and several other PQQ-dependent enzymes has remained controversial because of the absence of comprehensive structural data. We have determined the crystal structure of a ternary complex of s-GDH with PQQ and methylhydrazine, a competitive inhibitor of the enzyme. This complex, refined at 1.5-A resolution to an R factor of 16.7%, affords a detailed view of a cofactor-binding site of s-GDH. Moreover, it presents the first direct observation of covalent PQQ adduct in the active-site of a PQQ-dependent enzyme, thereby confirming previous evidence that the C5 carbonyl group of the cofactor is the most reactive moiety of PQQ.
About this Structure
1CRU is a Single protein structure of sequence from Acinetobacter calcoaceticus. Full crystallographic information is available from OCA.
Reference
Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: a covalent cofactor-inhibitor complex., Oubrie A, Rozeboom HJ, Dijkstra BW, Proc Natl Acad Sci U S A. 1999 Oct 12;96(21):11787-91. PMID:10518528 Page seeded by OCA on Fri May 2 13:02:59 2008