2bje
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(New page: 200px<br /> <applet load="2bje" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bje, resolution 1.90Å" /> '''ACYLPHOSPHATASE FRO...)
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Revision as of 18:13, 29 October 2007
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ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS. MONCLINIC P21 SPACE GROUP
Overview
The structure of AcP from the hyperthermophilic archaeon Sulfolobus, solfataricus has been determined by (1)H-NMR spectroscopy and X-ray, crystallography. Solution and crystal structures (1.27 A resolution, R-factor 13.7%) were obtained on the full-length protein and on an, N-truncated form lacking the first 12 residues, respectively. The overall, Sso AcP fold, starting at residue 13, displays the same, betaalphabetabetaalphabeta topology previously described for other members, of the AcP family from mesophilic sources. The unstructured N-terminal, tail may be crucial for the unusual aggregation mechanism of Sso AcP, previously reported. Sso AcP catalytic activity is reduced at room, temperature but rises at its working temperature to values comparable to, those displayed by its ... [(full description)]
About this Structure
2BJE is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with SO4 and CL as [ligands]. Active as [[1]], with EC number [3.6.1.7]. Full crystallographic information is available from [OCA].
Reference
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus., Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P, Proteins. 2006 Jan 1;62(1):64-79. PMID:16287076
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