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302 a.a.
_MG
Key reference
DOI no: 10.1107/S0907444903012629 Acta Crystallogr D Biol Crystallogr 59:1447-1453 (2003) PubMed id: 12876348
Structure of xylanase Xys1delta from Streptomyces halstedii. A.Canals, M.C.Vega, F.X.Gomis-Rüth, M.Díaz, R.I.Santamaría R, M.Coll. ABSTRACT
Xylanases hydrolyze the beta-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 A resolution with an R(merge) of 4.4%. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 A. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (beta/alpha)(8) barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.
Selected figure(s)
Figure 2.
Figure 2 Ribbon representation of Xys1. For clarity, only the major secondary-structure elements forming the (
/
)[8] barrel have been labelled. Additional minor helices are coloured orange. (a) Side view of the catalytic domain, with the carbonyl side of the
Figure 4.
Figure 4 Stereoviews of four structural details in the Xys1level.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1447-1453) copyright 2003. Figures were selected by the author.
Literature references that cite this PDB file's key reference
PubMed id Reference
16823036 K.Manikandan, A.Bhardwaj, N.Gupta, N.K.Lokanath, A.Ghosh, V.S.Reddy, and S.Ramakumar (2006).
Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditions.Protein Sci, 15, 1951-1960.
PDB codes: 2f8q 2fgl
16247799 Ihsanawati, T.Kumasaka, T.Kaneko, C.Morokuma, R.Yatsunami, T.Sato, S.Nakamura, and N.Tanaka (2005).
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8.Proteins, 61, 999.
PDB codes: 1vbr 1vbu
15522513 M.Díaz, S.Rodriguez, J.M.Fernández-Abalos, J.De Las Rivas, A.Ruiz-Arribas, V.L.Shnyrov, and R.I.Santamaría (2004).
Single mutations of residues outside the active center of the xylanase Xys1 Delta from Streptomyces halstedii JM8 affect its activity.FEMS Microbiol Lett, 240, 237-243. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.
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