2hw4

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[[Image:2hw4.gif|left|200px]]
[[Image:2hw4.gif|left|200px]]
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{{Structure
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|PDB= 2hw4 |SIZE=350|CAPTION= <scene name='initialview01'>2hw4</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_2hw4", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= PHPT1, PHP14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2hw4| PDB=2hw4 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hw4 OCA], [http://www.ebi.ac.uk/pdbsum/2hw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hw4 RCSB]</span>
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'''Crystal structure of human phosphohistidine phosphatase'''
'''Crystal structure of human phosphohistidine phosphatase'''
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[[Category: Uppenberg, J.]]
[[Category: Uppenberg, J.]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
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[[Category: human]]
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[[Category: Human]]
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[[Category: phosphatase]]
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[[Category: Phosphatase]]
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[[Category: phosphohistidine]]
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[[Category: Phosphohistidine]]
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[[Category: phpt1]]
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[[Category: Phpt1]]
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[[Category: sgc]]
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[[Category: Sgc]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural genomics consortium]]
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[[Category: Structural genomics consortium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:47:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:36:15 2008''
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Revision as of 03:47, 4 May 2008

Image:2hw4.gif

Template:STRUCTURE 2hw4

Crystal structure of human phosphohistidine phosphatase


Overview

Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. The structure of phosphohistidine phosphatase (PHPT1), the first identified eukaryotic-protein histidine phosphatase, has been determined to a resolution of 1.9A using multiple-wavelength anomalous dispersion methods. This enzyme can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues. Histidine 53 is proposed to play a major role in histidine dephosphorylation based on these observations and previous mutational studies. Models of peptide binding are discussed to suggest possible mechanisms for substrate recognition.

About this Structure

2HW4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

First structure of a eukaryotic phosphohistidine phosphatase., Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Hallberg BM, J Biol Chem. 2006 Nov 10;281(45):33830-4. Epub 2006 Sep 21. PMID:16990267 Page seeded by OCA on Sun May 4 06:47:07 2008

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