2g1a

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{{STRUCTURE_2g1a| PDB=2g1a | SCENE= }}
{{STRUCTURE_2g1a| PDB=2g1a | SCENE= }}
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'''Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase'''
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===Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase===
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==Overview==
 
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AphA is a periplasmic acid phosphatase of Escherichia coli belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. The crystal structure of AphA has been determined at 2.2A and its resolution extended to 1.7A on an AuCl(3) derivative. This represents the first crystal structure of a class B bacterial phosphatase. Despite the lack of sequence homology, the AphA structure reveals a haloacid dehalogenase-like fold. This finding suggests that this fold could be conserved among members of the DDDD superfamily of phosphohydrolases. The active enzyme is a homotetramer built by using an extended N-terminal arm intertwining the four monomers. The active site of the native enzyme, as prepared, hosts a magnesium ion, which can be replaced by other metal ions. The structure explains the non-specific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism.
 
==About this Structure==
==About this Structure==
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2G1A 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=2G1A OCA].
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2G1A is a 2 chains structure of sequences 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=2G1A OCA].
==Reference==
==Reference==
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The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold., Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Maria Rossolini G, Mangani S, J Mol Biol. 2004 Jan 16;335(3):761-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14687572 14687572]
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<ref group="xtra">PMID:14687572</ref><ref group="xtra">PMID:16330049</ref><references group="xtra"/>
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
 
[[Category: Benvenuti, M.]]
[[Category: Benvenuti, M.]]
[[Category: Calderone, V.]]
[[Category: Calderone, V.]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Metallo phosphatase]]
[[Category: Metallo phosphatase]]
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Revision as of 16:42, 16 February 2009

Template:STRUCTURE 2g1a

Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase

About this Structure

2G1A is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Maria Rossolini G, Mangani S. The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold. J Mol Biol. 2004 Jan 16;335(3):761-73. PMID:14687572
  • Calderone V, Forleo C, Benvenuti M, Thaller MC, Rossolini GM, Mangani S. A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases. J Mol Biol. 2006 Jan 27;355(4):708-21. Epub 2005 Nov 10. PMID:16330049 doi:http://dx.doi.org/10.1016/j.jmb.2005.10.068

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