2gv1

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[[Image:2gv1.jpg|left|200px]]
[[Image:2gv1.jpg|left|200px]]
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{{Structure
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|PDB= 2gv1 |SIZE=350|CAPTION= <scene name='initialview01'>2gv1</scene>
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The line below this paragraph, containing "STRUCTURE_2gv1", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylphosphatase Acylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7] </span>
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|GENE= yccX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2gv1| PDB=2gv1 | SCENE= }}
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|RELATEDENTRY=[[1y9o|1Y9O]], [[2acy|2ACY]], [[1aps|1APS]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gv1 OCA], [http://www.ebi.ac.uk/pdbsum/2gv1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gv1 RCSB]</span>
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'''NMR solution structure of the Acylphosphatase from Eschaerichia Coli'''
'''NMR solution structure of the Acylphosphatase from Eschaerichia Coli'''
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[[Category: Pagano, K.]]
[[Category: Pagano, K.]]
[[Category: Viglino, P.]]
[[Category: Viglino, P.]]
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[[Category: globular alpha-helix/beta-sheet protein]]
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[[Category: Globular alpha-helix/beta-sheet protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:34:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:22:00 2008''
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Revision as of 02:34, 4 May 2008

Image:2gv1.jpg

Template:STRUCTURE 2gv1

NMR solution structure of the Acylphosphatase from Eschaerichia Coli


Overview

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.

About this Structure

2GV1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

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:17021943 Page seeded by OCA on Sun May 4 05:34:24 2008

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