3VMV

Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165

Summary for 3VMV

• Entry DOI: 10.2210/pdb3vmv/pdb
• Related: 3VMW
• Descriptor: Pectate lyase, SULFATE ION (3 entities in total)
• Functional Keywords: polysaccharide lyase family 1, beta-helix, pectolytic, polygalacturonate, lyase
• Biological source: Bacillus
• Total number of polymer chains: 1
• Total formula weight: 36171.26

Authors

Zheng, Y.,Huang, C.H.,Liu, W.,Ko, T.P.,Xue, Y.,Zhou, C.,Zhang, G.,Guo, R.T.,Ma, Y. (deposition date: 2011-12-16, release date: 2012-07-25, Last modification date: 2023-11-08)

Primary citation

Zheng, Y.,Huang, C.H.,Liu, W.,Ko, T.P.,Xue, Y.,Zhou, C.,Guo, R.T.,Ma, Y.
Crystal structure and substrate-binding mode of a novel pectate lyase from alkaliphilic Bacillus sp. N16-5.
Biochem.Biophys.Res.Commun., 420:269-274, 2012

PubMed Abstract: The pectate lyase (Bsp165PelA) from Bacillus sp. N16-5 has great potential in industrial applications because it shows high specific activity under extremely alkaline conditions. Besides, activity measurement of Bsp165PelA does not require addition of calcium, in a way different from the other pectate lyases. Here we report crystal structures of Bsp165PelA in apo-form and in complex with trigalacturonate. The parallel β-helix, active site residues and substrate binding cleft are similar to those in the other pectate lyases from Polysaccharide Lyase family 1. However, some of the highly conserved Ca(2+) binding residues and secondary structures are altered in Bsp165PelA, making it difficult to coordinate with Ca(2+) as in the other pectate lyases. We found Bsp165PelA forms some direct enzyme-substrate interactions instead of using Ca(2+) ions bridging in the extremely alkaline environment.

PubMed: 22414692
DOI: 10.1016/j.bbrc.2012.02.148

Experimental method

X-RAY DIFFRACTION (1.54 Å)