2gv1: Difference between revisions

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[[Image:2gv1.jpg|left|200px]]
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[[Image:2gv1.png|left|200px]]


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{{STRUCTURE_2gv1|  PDB=2gv1  |  SCENE=  }}  
{{STRUCTURE_2gv1|  PDB=2gv1  |  SCENE=  }}  


'''NMR solution structure of the Acylphosphatase from Eschaerichia Coli'''
===NMR solution structure of the Acylphosphatase from Eschaerichia Coli===




==Overview==
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The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.
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==About this Structure==
==About this Structure==
2GV1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV1 OCA].  
2GV1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GV1 OCA].  


==Reference==
==Reference==
NMR solution structure of the acylphosphatase from Escherichia coli., Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A, J Biomol NMR. 2006 Nov;36(3):199-204. Epub 2006 Oct 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17021943 17021943]
NMR solution structure of the acylphosphatase from Escherichia coli., Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A, J Biomol NMR. 2006 Nov;36(3):199-204. Epub 2006 Oct 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17021943 17021943]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16287076 16287076]
Crystal structure of common type acylphosphatase from bovine testis., Thunnissen MM, Taddei N, Liguri G, Ramponi G, Nordlund P, Structure. 1997 Jan 15;5(1):69-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9016712 9016712]
Three-dimensional structure of acylphosphatase. Refinement and structure analysis., Pastore A, Saudek V, Ramponi G, Williams RJ, J Mol Biol. 1992 Mar 20;224(2):427-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1313885 1313885]
[[Category: Acylphosphatase]]
[[Category: Acylphosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Viglino, P.]]
[[Category: Viglino, P.]]
[[Category: Globular alpha-helix/beta-sheet protein]]
[[Category: Globular alpha-helix/beta-sheet protein]]
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