2g1a
From Proteopedia
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| - | [[Image:2g1a.jpg|left|200px]] | + | [[Image:2g1a.jpg|left|200px]] |
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| - | '''Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase''' | + | {{Structure |
| + | |PDB= 2g1a |SIZE=350|CAPTION= <scene name='initialview01'>2g1a</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=5HG:{[2-(6-AMINO-9H-PURIN-9-YL)ETHOXY]METHYL}PHOSPHONIC ACID'>5HG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] | ||
| + | |GENE= aphA, napA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2G1A is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Acid phosphatase]] | [[Category: Acid phosphatase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: hydrolase; acid phosphatase/phosphotransferase; metallo phosphatase]] | [[Category: hydrolase; acid phosphatase/phosphotransferase; metallo phosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:59:13 2008'' |
Revision as of 14:59, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | and | ||||||
| Gene: | aphA, napA (Escherichia coli) | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase
Overview
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
2G1A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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:14687572
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