1g72: Difference between revisions

Revision as of 13:46, 21 February 2008

CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION

OverviewOverview

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 StructureAbout this Structure

1G72 is a Protein complex structure of sequences from Methylophilus methylotrophus with and as ligands. This structure supersedes the now removed PDB entry 1B2N. Active as Alcohol dehydrogenase (acceptor), with EC number 1.1.99.8 Full crystallographic information is available from OCA.

ReferenceReference

Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation., Zheng YJ, Xia Zx, Chen Zw, Mathews FS, Bruice TC, Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):432-4. Epub 2001 Jan 9. PMID:11149955

Page seeded by OCA on Thu Feb 21 12:46:51 2008

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OCA

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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;" />
 '''CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''<br />
 ==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==
-G72 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].
+G72 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==
@@ Line 14: / Line 14: @@
 [[Category: Methylophilus methylotrophus]]
 [[Category: Protein complex]]
-[[Category: Bruice, T.C.]]
+[[Category: Bruice, T C.]]
 [[Category: Chen, Z.]]
-[[Category: Mathews, F.S.]]
+[[Category: Mathews, F S.]]
 [[Category: Xia, Z.]]
 [[Category: Zheng, Y.]]
@@ Line 23: / Line 23: @@
 [[Category: quinoprotein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:46:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:51 2008''