1kdg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1kdg |SIZE=350|CAPTION= <scene name='initialview01'>1kdg</scene>, resolution 1.50&Aring;
|PDB= 1kdg |SIZE=350|CAPTION= <scene name='initialview01'>1kdg</scene>, resolution 1.50&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=6FA:6-HYDROXY-FLAVIN-ADENINE+DINUCLEOTIDE'>6FA</scene>, <scene name='pdbligand=EMT:2-(ETHYLMERCURI-THIO)-BENZOIC+ACID'>EMT</scene> and <scene name='pdbligand=S:SULFUR ATOM'>S</scene>
+
|LIGAND= <scene name='pdbligand=6FA:6-HYDROXY-FLAVIN-ADENINE+DINUCLEOTIDE'>6FA</scene>, <scene name='pdbligand=EMT:2-(ETHYLMERCURI-THIO)-BENZOIC+ACID'>EMT</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=S:SULFUR+ATOM'>S</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1d7b|1D7B]], [[1d7c|1D7C]], [[1d7d|1D7D]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdg OCA], [http://www.ebi.ac.uk/pdbsum/1kdg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kdg RCSB]</span>
}}
}}
Line 26: Line 29:
[[Category: Henriksson, G.]]
[[Category: Henriksson, G.]]
[[Category: Pettersson, G.]]
[[Category: Pettersson, G.]]
-
[[Category: 6FA]]
 
-
[[Category: EMT]]
 
-
[[Category: HG]]
 
-
[[Category: MAN]]
 
-
[[Category: NAG]]
 
-
[[Category: S]]
 
[[Category: 6-hydroxylated fad]]
[[Category: 6-hydroxylated fad]]
[[Category: alpha/beta structure]]
[[Category: alpha/beta structure]]
Line 38: Line 35:
[[Category: rossmann fold]]
[[Category: rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:15:53 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:46:57 2008''

Revision as of 18:46, 30 March 2008


PDB ID 1kdg

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: , , , , ,
Related: 1D7B, 1D7C, 1D7D


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Sun Mar 30 21:46:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools