5amv

Structural insights into the loss of catalytic competence in pectate lyase at low pH

spinqualitylabelsall models 5amv, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5amv is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Ligands: ACT, ADA, CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLY_BACSU Produces unsaturated products from polygalacturonate. Publication Abstract from PubMed Pectate lyase, a family 1 polysaccharide lyase, catalyses cleavage of the alpha-1,4 linkage of the polysaccharide homogalacturonan via an anti beta-elimination reaction. In the Michaelis complex two calcium ions bind between the C6 carboxylate of the d-galacturonate residue and enzyme aspartates at the active centre (+1 subsite), they withdraw electrons acidifying the C5 proton facilitating its abstraction by the catalytic arginine. Here we show that activity is lost at low pH because protonation of aspartates results in the loss of the two catalytic calcium-ions causing a profound failure to correctly organise the Michaelis complex. Structural insights into the loss of catalytic competence in pectate lyase activity at low pH.,Ali S, Sondergaard CR, Teixeira S, Pickersgill RW FEBS Lett. 2015 Sep 28. pii: S0014-5793(15)00838-8. doi:, 10.1016/j.febslet.2015.09.014. PMID:26420545 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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