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2bje

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{{STRUCTURE_2bje| PDB=2bje | SCENE= }}
{{STRUCTURE_2bje| PDB=2bje | SCENE= }}
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'''ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS. MONCLINIC P21 SPACE GROUP'''
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===ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS. MONCLINIC P21 SPACE GROUP===
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==Overview==
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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 mesophilic counterparts at 25-37 degrees C. Such a reduced activity can result from protein rigidity and from the active site stiffening due the presence of a salt bridge between the C-terminal carboxylate and the active site arginine. Sso AcP is characterized by a melting temperature, Tm, of 100.8 degrees C and an unfolding free energy, DeltaG(U-F)H2O, at 28 degrees C and 81 degrees C of 48.7 and 20.6 kJ mol(-1), respectively. The kinetic and structural data indicate that mesophilic and hyperthermophilic AcP's display similar enzymatic activities and conformational stabilities at their working conditions. Structural analysis of the factor responsible for Sso AcP thermostability with respect to mesophilic AcP's revealed the importance of a ion pair network stabilizing particularly the beta-sheet and the loop connecting the fourth and fifth strands, together with increased density packing, loop shortening and a higher alpha-helical propensity.
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{{ABSTRACT_PUBMED_16287076}}
==About this Structure==
==About this Structure==
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[[Category: Zuccotti, S.]]
[[Category: Zuccotti, S.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 07:09, 29 July 2008

Image:2bje.png

Template:STRUCTURE 2bje

ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS. MONCLINIC P21 SPACE GROUP

Template:ABSTRACT PUBMED 16287076

About this Structure

2BJE is a Single protein structure of sequence from Sulfolobus solfataricus. 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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