1V6U

Crystal Structure Of Xylanase From Streptomyces Olivaceoviridis E-86 Complexed With 2(2)-alpha-L-arabinofuranosyl-xylobiose

Summary for 1V6U

• Entry DOI: 10.2210/pdb1v6u/pdb
• Related: 1V6V 1V6W 1V6X 1isw 1xyf
• Related PRD ID: PRD_900116
• Descriptor: endo-1,4-beta-D-xylanase, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, alpha-L-arabinofuranose-(1-3)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, ... (6 entities in total)
• Functional Keywords: alpha-beta barrel, protein-sugar complex, carbohydrate binding module, hydrolase
• Biological source: Streptomyces olivaceoviridis
• Total number of polymer chains: 2
• Total formula weight: 95990.54

Authors

Fujimoto, Z.,Kaneko, S.,Kuno, A.,Kobayashi, H.,Kusakabe, I.,Mizuno, H. (deposition date: 2003-12-04, release date: 2004-04-27, Last modification date: 2023-10-25)

Primary citation

Fujimoto, Z.,Kaneko, S.,Kuno, A.,Kobayashi, H.,Kusakabe, I.,Mizuno, H.
Crystal structures of decorated xylooligosaccharides bound to a family 10 xylanase from Streptomyces olivaceoviridis E-86
J.Biol.Chem., 279:9606-9614, 2004

PubMed Abstract: The family 10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) consists of a GH10 catalytic domain, which is joined by a Gly/Pro-rich linker to a family 13 carbohydrate-binding module (CBM13) that interacts with xylan. To understand how GH10 xylanases and CBM13 recognize decorated xylans, the crystal structure of SoXyn10A was determined in complex with alpha-l-arabinofuranosyl- and 4-O-methyl-alpha-d-glucuronosyl-xylooligosaccharides. The bound sugars were observed in the subsites of the catalytic cleft and also in subdomains alpha and gamma of CBM13. The data reveal that the binding mode of the oligosaccharides in the active site of the catalytic domain is entirely consistent with the substrate specificity and, in conjunction with the accompanying paper, demonstrate that the accommodation of the side chains in decorated xylans is conserved in GH10 xylanases of SoXyn10A against arabinoglucuronoxylan. CBM13 was shown to bind xylose or xylooligosaccharides reversibly by using nonsymmetric sugars as the ligands. The independent multiple sites in CBM13 may increase the probability of substrate binding.

PubMed: 14670957
DOI: 10.1074/jbc.M312293200

Experimental method

X-RAY DIFFRACTION (2.1 Å)