2hw4
From Proteopedia
(New page: 200px<br /> <applet load="2hw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hw4, resolution 1.90Å" /> '''Crystal structure o...) |
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| - | [[Image:2hw4.gif|left|200px]]<br /> | + | [[Image:2hw4.gif|left|200px]]<br /><applet load="2hw4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2hw4" size=" | + | |
caption="2hw4, resolution 1.90Å" /> | caption="2hw4, resolution 1.90Å" /> | ||
'''Crystal structure of human phosphohistidine phosphatase'''<br /> | '''Crystal structure of human phosphohistidine phosphatase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphatases are a diverse group of enzymes that regulate numerous | + | 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== | ==About this Structure== | ||
| - | 2HW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FMT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2HW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HW4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Arrowsmith, C.]] | [[Category: Arrowsmith, C.]] | ||
| - | [[Category: Berg, S | + | [[Category: Berg, S Van Den.]] |
[[Category: Berglund, H.]] | [[Category: Berglund, H.]] | ||
| - | [[Category: Busam, R | + | [[Category: Busam, R D.]] |
[[Category: Collins, R.]] | [[Category: Collins, R.]] | ||
[[Category: Edwards, A.]] | [[Category: Edwards, A.]] | ||
| Line 24: | Line 23: | ||
[[Category: Flores, A.]] | [[Category: Flores, A.]] | ||
[[Category: Graslund, S.]] | [[Category: Graslund, S.]] | ||
| - | [[Category: Hallberg, B | + | [[Category: Hallberg, B M.]] |
[[Category: Hammarstrom, M.]] | [[Category: Hammarstrom, M.]] | ||
[[Category: Hogbom, M.]] | [[Category: Hogbom, M.]] | ||
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[[Category: Ogg, D.]] | [[Category: Ogg, D.]] | ||
[[Category: Persson, C.]] | [[Category: Persson, C.]] | ||
| - | [[Category: SGC, Structural | + | [[Category: SGC, Structural Genomics Consortium.]] |
| - | [[Category: Schiavone, L | + | [[Category: Schiavone, L Holmberg.]] |
[[Category: Stenmark, P.]] | [[Category: Stenmark, P.]] | ||
[[Category: Sundstrom, M.]] | [[Category: Sundstrom, M.]] | ||
| - | [[Category: Thorsell, A | + | [[Category: Thorsell, A G.]] |
[[Category: Uppenberg, J.]] | [[Category: Uppenberg, J.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:46:20 2008'' |
Revision as of 15:46, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 17:46:20 2008
Categories: Homo sapiens | Single protein | Arrowsmith, C. | Berg, S Van Den. | Berglund, H. | Busam, R D. | Collins, R. | Edwards, A. | Ehn, M. | Flodin, S. | Flores, A. | Graslund, S. | Hallberg, B M. | Hammarstrom, M. | Hogbom, M. | Kotenyova, T. | Nilsson-Ehle, P. | Nordlund, P. | Nyman, T. | Ogg, D. | Persson, C. | SGC, Structural Genomics Consortium. | Schiavone, L Holmberg. | Stenmark, P. | Sundstrom, M. | Thorsell, A G. | Uppenberg, J. | Weigelt, J. | FMT | Human | Phosphatase | Phosphohistidine | Phpt1 | Sgc | Structural genomics | Structural genomics consortium
