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2XQX

Structure of the family 32 carbohydrate-binding module from Streptococcus pneumoniae EndoD

Summary for 2XQX
Entry DOI10.2210/pdb2xqx/pdb
Related2W91 2W92
DescriptorENDO-BETA-N-ACETYLGLUCOSAMINIDASE D, CALCIUM ION, ACETATE ION, ... (4 entities in total)
Functional Keywordssugar binding protein, carbohydrate binding, beta-sandwhich
Biological sourceSTREPTOCOCCUS PNEUMONIAE
Cellular locationSecreted, cell wall; Peptidoglycan-anchor (By similarity): Q93HW0
Total number of polymer chains2
Total formula weight34118.66
Authors
Abbott, D.W.,Boraston, A.B. (deposition date: 2010-09-07, release date: 2010-11-03, Last modification date: 2024-10-23)
Primary citationAbbott, D.W.,Boraston, A.B.
Structural Analysis of a Putative Family 32 Carbohydrate-Binding Module from the Streptococcus Pneumoniae Enzyme Endod.
Acta Crystallogr.,Sect.F, 67:429-, 2011
Cited by
PubMed Abstract: EndoD is an architecturally complex endo-β-1,4-N-acetylglucosamidase from Streptococcus pneumoniae that cleaves the chitobiose core of N-linked glycans and contributes to pneumococcal virulence. Although the glycoside hydrolase family 85 catalytic module has been structurally and functionally characterized, nothing is known about the ancillary modules and how they contribute to the overall function of the enzyme. Presented here is the 2.0 Å resolution structure of a family 32 carbohydrate-binding module of EndoD, SpCBM32, solved by single-wavelength anomalous dispersion. The putative binding site of this protein is a charge-neutral relatively flat region on the protein surface that contains one prominently exposed tryptophan residue that extends into the solvent. These topographical features are discussed in the biological context of EndoD activity and a hypothesis is made about the complex structure of its potential carbohydrate ligand.
PubMed: 21505233
DOI: 10.1107/S1744309111001874
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

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