1g72: Difference between revisions

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New page: left|200px<br /><applet load="1g72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g72, resolution 1.90Å" /> '''CATALYTIC MECHANISM ...
 
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[[Image:1g72.jpg|left|200px]]<br /><applet load="1g72" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g72.jpg|left|200px]]<br /><applet load="1g72" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g72, resolution 1.90&Aring;" />
caption="1g72, resolution 1.90&Aring;" />
'''CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''<br />
'''CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''<br />


==Overview==
==Overview==
The catalytic mechanism of the reductive half reaction of the quinoprotein, methanol dehydrogenase (MDH) is believed to proceed either through a, hemiketal intermediate or by direct transfer of a hydride ion from the, substrate methyl group to the cofactor, pyrroloquinoline quinone (PQQ). A, crystal structure of the enzyme-substrate complex of a similar, quinoprotein, glucose dehydrogenase, has recently been reported that, strongly favors the hydride transfer mechanism in that enzyme. A, theoretical analysis and an improved refinement of the 1.9-A resolution, crystal structure of MDH from Methylophilus methylotrophus W3A1 in the, presence of methanol, reported earlier, indicates that the observed, tetrahedral configuration of the C-5 atom of PQQ in that study represents, the C-5-reduced form of the cofactor and lends support for a hydride, transfer mechanism for MDH.
The catalytic mechanism of the reductive half reaction of the quinoprotein methanol dehydrogenase (MDH) is believed to proceed either through a hemiketal intermediate or by direct transfer of a hydride ion from the substrate methyl group to the cofactor, pyrroloquinoline quinone (PQQ). A crystal structure of the enzyme-substrate complex of a similar quinoprotein, glucose dehydrogenase, has recently been reported that strongly favors the hydride transfer mechanism in that enzyme. A theoretical analysis and an improved refinement of the 1.9-A resolution crystal structure of MDH from Methylophilus methylotrophus W3A1 in the presence of methanol, reported earlier, indicates that the observed tetrahedral configuration of the C-5 atom of PQQ in that study represents the C-5-reduced form of the cofactor and lends support for a hydride transfer mechanism for MDH.


==About this Structure==
==About this Structure==
1G72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus] with CA and PQQ as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1B2N. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor) Alcohol dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G72 OCA].  
1G72 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PQQ:'>PQQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1B2N. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor) Alcohol dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G72 OCA].  


==Reference==
==Reference==
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[[Category: Methylophilus methylotrophus]]
[[Category: Methylophilus methylotrophus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bruice, T.C.]]
[[Category: Bruice, T C.]]
[[Category: Chen, Z.]]
[[Category: Chen, Z.]]
[[Category: Mathews, F.S.]]
[[Category: Mathews, F S.]]
[[Category: Xia, Z.]]
[[Category: Xia, Z.]]
[[Category: Zheng, Y.]]
[[Category: Zheng, Y.]]
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[[Category: quinoprotein]]
[[Category: quinoprotein]]


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