2d0v

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[[Image:2d0v.gif|left|200px]]<br /><applet load="2d0v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2d0v.gif|left|200px]]
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caption="2d0v, resolution 2.49&Aring;" />
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'''Crystal structure of methanol dehydrogenase from Hyphomicrobium denitrificans'''<br />
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{{Structure
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|PDB= 2d0v |SIZE=350|CAPTION= <scene name='initialview01'>2d0v</scene>, resolution 2.49&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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'''Crystal structure of methanol dehydrogenase from Hyphomicrobium denitrificans'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2D0V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hyphomicrobium_denitrificans Hyphomicrobium denitrificans] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PQQ:'>PQQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2D0V OCA].
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2D0V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hyphomicrobium_denitrificans Hyphomicrobium denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D0V OCA].
==Reference==
==Reference==
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Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins., Nojiri M, Hira D, Yamaguchi K, Okajima T, Tanizawa K, Suzuki S, Biochemistry. 2006 Mar 21;45(11):3481-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16533029 16533029]
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Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins., Nojiri M, Hira D, Yamaguchi K, Okajima T, Tanizawa K, Suzuki S, Biochemistry. 2006 Mar 21;45(11):3481-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16533029 16533029]
[[Category: Alcohol dehydrogenase (acceptor)]]
[[Category: Alcohol dehydrogenase (acceptor)]]
[[Category: Hyphomicrobium denitrificans]]
[[Category: Hyphomicrobium denitrificans]]
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[[Category: pqq]]
[[Category: pqq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:07 2008''

Revision as of 14:22, 20 March 2008


PDB ID 2d0v

Drag the structure with the mouse to rotate
, resolution 2.49Å
Ligands: and
Activity: Alcohol dehydrogenase (acceptor), with EC number 1.1.99.8
Coordinates: save as pdb, mmCIF, xml



Crystal structure of methanol dehydrogenase from Hyphomicrobium denitrificans


Overview

Methanol dehydrogenase (Hd-MDH) and its physiological electron acceptor, cytochrome c(L) (Hd-Cyt c(L)), isolated from a methylotrophic denitrifying bacterium, Hyphomicrobium denitrificans A3151, have been kinetically and structurally characterized; the X-ray structures of Hd-MDH and Hd-Cyt c(L) have been determined using molecular replacement at 2.5 and 2.0 A resolution, respectively. To explain the mechanism for electron transfer between these proteins, the dependence of MDH activity on the concentration of Hd-Cyt c(L) has been investigated at pH 4.5-7.0. The Michaelis constant for Hd-Cyt c(L) shows the smallest value (approximately 0.3 microM) at pH 5.5. The pseudo-first-order rate constant (k(obs)) of the reduction of Hd-Cyt c(L) exhibits a hyperbolic concentration dependence of Hd-MDH at pH 5.5, although k(obs) linearly increases at pH 6.5. These findings indicate formation of a transient complex between these proteins during an electron transfer event. Hd-MDH (148 kDa) is a large tetrameric protein with an alpha(2)beta(2) subunit composition, showing a high degree of structural similarity with other MDHs. Hd-Cyt c(L) (19 kDa) exhibiting the alpha-band at 550.7 nm has a unique C-terminal region involving a disulfide bond between Cys47 and Cys165. Moreover, there is a pair of Hd-Cyt c(L) monomers related with a pseudo-2-fold axis of symmetry in the asymmetric unit, and the two monomers tightly interact with each other through three hydrogen bonds. This configuration is the first example in the studies of cytochrome c as the physiological electron acceptor for MDH. The docking simulation between the coupled Hd-Cyt c(L) molecules and the heterotetrameric Hd-MDH molecule has been carried out.

About this Structure

2D0V is a Protein complex structure of sequences from Hyphomicrobium denitrificans. Full crystallographic information is available from OCA.

Reference

Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins., Nojiri M, Hira D, Yamaguchi K, Okajima T, Tanizawa K, Suzuki S, Biochemistry. 2006 Mar 21;45(11):3481-92. PMID:16533029

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