1kdg

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(New page: 200px<br /><applet load="1kdg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdg, resolution 1.50&Aring;" /> '''Crystal structure of...)
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caption="1kdg, resolution 1.50&Aring;" />
caption="1kdg, resolution 1.50&Aring;" />
'''Crystal structure of the flavin domain of cellobiose dehydrogenase'''<br />
'''Crystal structure of the flavin domain of cellobiose dehydrogenase'''<br />
==Overview==
==Overview==
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Cellobiose dehydrogenase (CDH) participates in the degradation of, cellulose and lignin. The protein is an extracellular flavocytochrome with, a b-type cytochrome domain (CYT(cdh)) connected to a flavodehydrogenase, domain (DH(cdh)). DH(cdh) catalyses a two-electron oxidation at the, anomeric C1 position of cellobiose to yield cellobiono-1,5-lactone, and, the electrons are subsequently transferred from DH(cdh) to an acceptor, either directly or via CYT(cdh). Here, we describe the crystal structure, of Phanerochaete chrysosporium DH(cdh) determined at 1.5 A resolution., DH(cdh) belongs to the GMC family of oxidoreductases, which includes, glucose oxidase (GOX) and cholesterol oxidase (COX); however, the sequence, identity with members of the family is low. The overall fold of DH(cdh) is, p-hydroxybenzoate hydroxylase-like and is similar to, but also different, from, that of GOX and COX. It is partitioned into an FAD-binding subdomain, of alpha/beta type and a substrate-binding subdomain consisting of a, seven-stranded beta sheet and six helices. Docking of CYT(cdh) and DH(cdh), suggests that CYT(cdh) covers the active-site entrance in DH(cdh), and, that the resulting distance between the cofactors is within acceptable, limits for inter-domain electron transfer. Based on docking of the, substrate, cellobiose, in the active site of DH(cdh), we propose that the, enzyme discriminates against glucose by favouring interaction with the, non-reducing end of cellobiose.
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Cellobiose dehydrogenase (CDH) participates in the degradation of cellulose and lignin. The protein is an extracellular flavocytochrome with a b-type cytochrome domain (CYT(cdh)) connected to a flavodehydrogenase domain (DH(cdh)). DH(cdh) catalyses a two-electron oxidation at the anomeric C1 position of cellobiose to yield cellobiono-1,5-lactone, and the electrons are subsequently transferred from DH(cdh) to an acceptor, either directly or via CYT(cdh). Here, we describe the crystal structure of Phanerochaete chrysosporium DH(cdh) determined at 1.5 A resolution. DH(cdh) belongs to the GMC family of oxidoreductases, which includes glucose oxidase (GOX) and cholesterol oxidase (COX); however, the sequence identity with members of the family is low. The overall fold of DH(cdh) is p-hydroxybenzoate hydroxylase-like and is similar to, but also different from, that of GOX and COX. It is partitioned into an FAD-binding subdomain of alpha/beta type and a substrate-binding subdomain consisting of a seven-stranded beta sheet and six helices. Docking of CYT(cdh) and DH(cdh) suggests that CYT(cdh) covers the active-site entrance in DH(cdh), and that the resulting distance between the cofactors is within acceptable limits for inter-domain electron transfer. Based on docking of the substrate, cellobiose, in the active site of DH(cdh), we propose that the enzyme discriminates against glucose by favouring interaction with the non-reducing end of cellobiose.
==About this Structure==
==About this Structure==
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1KDG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium] with NAG, MAN, HG, 6FA, EMT and S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KDG OCA].
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1KDG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=6FA:'>6FA</scene>, <scene name='pdbligand=EMT:'>EMT</scene> and <scene name='pdbligand=S:'>S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDG OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Divne, C.]]
[[Category: Divne, C.]]
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[[Category: Hallberg, B.M.]]
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[[Category: Hallberg, B M.]]
[[Category: Henriksson, G.]]
[[Category: Henriksson, G.]]
[[Category: Pettersson, G.]]
[[Category: Pettersson, G.]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:04:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:50 2008''

Revision as of 11:32, 21 February 2008


1kdg, resolution 1.50Å

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Crystal structure of the flavin domain of cellobiose dehydrogenase

Overview

Cellobiose dehydrogenase (CDH) participates in the degradation of cellulose and lignin. The protein is an extracellular flavocytochrome with a b-type cytochrome domain (CYT(cdh)) connected to a flavodehydrogenase domain (DH(cdh)). DH(cdh) catalyses a two-electron oxidation at the anomeric C1 position of cellobiose to yield cellobiono-1,5-lactone, and the electrons are subsequently transferred from DH(cdh) to an acceptor, either directly or via CYT(cdh). Here, we describe the crystal structure of Phanerochaete chrysosporium DH(cdh) determined at 1.5 A resolution. DH(cdh) belongs to the GMC family of oxidoreductases, which includes glucose oxidase (GOX) and cholesterol oxidase (COX); however, the sequence identity with members of the family is low. The overall fold of DH(cdh) is p-hydroxybenzoate hydroxylase-like and is similar to, but also different from, that of GOX and COX. It is partitioned into an FAD-binding subdomain of alpha/beta type and a substrate-binding subdomain consisting of a seven-stranded beta sheet and six helices. Docking of CYT(cdh) and DH(cdh) suggests that CYT(cdh) covers the active-site entrance in DH(cdh), and that the resulting distance between the cofactors is within acceptable limits for inter-domain electron transfer. Based on docking of the substrate, cellobiose, in the active site of DH(cdh), we propose that the enzyme discriminates against glucose by favouring interaction with the non-reducing end of cellobiose.

About this Structure

1KDG is a Single protein structure of sequence from Phanerochaete chrysosporium with , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase., Hallberg BM, Henriksson G, Pettersson G, Divne C, J Mol Biol. 2002 Jan 18;315(3):421-34. PMID:11786022

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