2XQX
Structure of the family 32 carbohydrate-binding module from Streptococcus pneumoniae EndoD
Summary for 2XQX
Entry DOI | 10.2210/pdb2xqx/pdb |
Related | 2W91 2W92 |
Descriptor | ENDO-BETA-N-ACETYLGLUCOSAMINIDASE D, CALCIUM ION, ACETATE ION, ... (4 entities in total) |
Functional Keywords | sugar binding protein, carbohydrate binding, beta-sandwhich |
Biological source | STREPTOCOCCUS PNEUMONIAE |
Cellular location | Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q93HW0 |
Total number of polymer chains | 2 |
Total formula weight | 34118.66 |
Authors | Abbott, D.W.,Boraston, A.B. (deposition date: 2010-09-07, release date: 2010-11-03, Last modification date: 2024-10-23) |
Primary citation | Abbott, 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: 21505233DOI: 10.1107/S1744309111001874 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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