1g72

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[[Image:1g72.jpg|left|200px]]<br /><applet load="1g72" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g72.jpg|left|200px]]
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caption="1g72, resolution 1.90&Aring;" />
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'''CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''<br />
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{{Structure
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|PDB= 1g72 |SIZE=350|CAPTION= <scene name='initialview01'>1g72</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=PQQ:PYRROLOQUINOLINE QUINONE'>PQQ</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1G72 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. This structure supersedes the now removed PDB entry 1B2N. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G72 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11149955 11149955]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11149955 11149955]
[[Category: Alcohol dehydrogenase (acceptor)]]
[[Category: Alcohol dehydrogenase (acceptor)]]
[[Category: Methylophilus methylotrophus]]
[[Category: Methylophilus methylotrophus]]
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[[Category: quinoprotein]]
[[Category: quinoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:19:06 2008''

Revision as of 09:19, 20 March 2008


PDB ID 1g72

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: and
Activity: Alcohol dehydrogenase (acceptor), with EC number 1.1.99.8
Coordinates: save as pdb, mmCIF, xml



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


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.

About this Structure

1G72 is a Protein complex structure of sequences from Methylophilus methylotrophus. This structure supersedes the now removed PDB entry 1B2N. Full crystallographic information is available from OCA.

Reference

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

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