1kv9

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(New page: 200px<br /><applet load="1kv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kv9, resolution 1.9&Aring;" /> '''Structure at 1.9 A Re...)
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[[Image:1kv9.jpg|left|200px]]<br /><applet load="1kv9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kv9, resolution 1.9&Aring;" />
caption="1kv9, resolution 1.9&Aring;" />
'''Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5'''<br />
'''Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5'''<br />
==Overview==
==Overview==
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The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida, is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde, and transfers electrons first to pyrroloquinoline quinone (PQQ) and then, to an internal heme group. The 1.9 A resolution crystal structure reveals, that the enzyme contains a large N-terminal eight-stranded beta propeller, domain (approximately 60 kDa) similar to methanol dehydrogenase and a, small C-terminal c-type cytochrome domain (approximately 10 kDa) similar, to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound, near the axis of the propeller domain about 14 A from the heme. A molecule, of acetone, the product of the oxidation of isopropanol present during, crystallization, appears to be bound in the active site cavity.
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The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 A resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (approximately 60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (approximately 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 A from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.
==About this Structure==
==About this Structure==
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1KV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with CA, PQQ, HEM, EPE, ACN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KV9 OCA].
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1KV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=PQQ:'>PQQ</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=EPE:'>EPE</scene>, <scene name='pdbligand=ACN:'>ACN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KV9 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Adachi, O.]]
[[Category: Adachi, O.]]
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[[Category: Bellamy, H.D.]]
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[[Category: Bellamy, H D.]]
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[[Category: Chen, Z.W.]]
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[[Category: Chen, Z W.]]
[[Category: Fujii, T.]]
[[Category: Fujii, T.]]
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[[Category: Mathews, F.S.]]
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[[Category: Mathews, F S.]]
[[Category: Matsushita, K.]]
[[Category: Matsushita, K.]]
[[Category: Toyama, H.]]
[[Category: Toyama, H.]]
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[[Category: quinohemoprotein alcohol dehydrogenase]]
[[Category: quinohemoprotein alcohol dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:00:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:15 2008''

Revision as of 11:38, 21 February 2008

Image:1kv9.jpg

1kv9, resolution 1.9Å

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Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5

Overview

The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 A resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (approximately 60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (approximately 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 A from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.

About this Structure

1KV9 is a Single protein structure of sequence from Pseudomonas putida with , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5., Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS, Structure. 2002 Jun;10(6):837-49. PMID:12057198

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