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2fhm
From Proteopedia
Revision as of 00:26, 30 September 2014 by OCA (Talk | contribs)
2fhm is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Acylphosphatase is a small enzyme that catalyzes the hydrolysis of acyl phosphates. Here, we present the solution structure of acylphosphatase from Bacillus subtilis (BsAcP), the first from a Gram-positive bacterium. We found that its active site is disordered, whereas it converted to an ordered state upon ligand binding. The structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH (pH<5.8). Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration. This study provides direct evidence for the role of ligand in conformational selection.
Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis.,Hu J, Li D, Su XD, Jin C, Xia B FEBS Lett. 2010 Jul 2;584(13):2852-6. Epub 2010 May 4. PMID:20447399[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Hu J, Li D, Su XD, Jin C, Xia B. Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis. FEBS Lett. 2010 Jul 2;584(13):2852-6. Epub 2010 May 4. PMID:20447399 doi:10.1016/j.febslet.2010.04.069
