4E4P
Second native structure of Xylanase A1 from Paenibacillus sp. JDR-2
Summary for 4E4P
| Entry DOI | 10.2210/pdb4e4p/pdb |
| Related | 3RDK 3RO8 |
| Descriptor | Endo-1,4-beta-xylanase A, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | xylanase, paenibacillus, tim barrel, beta/alpha 8 fold, hydrolase |
| Biological source | Paenibacillus sp. |
| Cellular location | Secreted, cell wall : C6CRV0 |
| Total number of polymer chains | 2 |
| Total formula weight | 76971.74 |
| Authors | Pozharski, E.,St John, F.J. (deposition date: 2012-03-13, release date: 2012-04-18, Last modification date: 2024-02-28) |
| Primary citation | St John, F.J.,Preston, J.F.,Pozharski, E. Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2. J.Struct.Biol., 180:303-311, 2012 Cited by PubMed Abstract: The Gram-positive bacterium Paenibacillus sp. JDR-2 (PbJDR2) has been shown to have novel properties in the utilization of the abundant but chemically complex hemicellulosic sugar glucuronoxylan. Xylanase A1 of PbJDR2 (PbXynA1) has been implicated in an efficient process in which extracellular depolymerization of this polysaccharide is coupled to assimilation and intracellular metabolism. PbXynA1is a 154kDa cell wall anchored multimodular glycosyl hydrolase family 10 (GH10) xylanase. In this work, the 38kDa catalytic module of PbXynA1 has been structurally characterized revealing several new features not previously observed in structures of GH10 xylanases. These features are thought to facilitate hydrolysis of highly substituted, chemically complex xylans that may be the form found in close proximity to the cell wall of PbJDR2, an organism shown to have a preference for growth on polymeric glucuronoxylan. PubMed: 23000703DOI: 10.1016/j.jsb.2012.09.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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