1nf2: Difference between revisions
New page: left|200px<br /><applet load="1nf2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nf2, resolution 2.20Å" /> '''X-ray crystal struct... |
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[[Image:1nf2.gif|left|200px]]<br /><applet load="1nf2" size=" | [[Image:1nf2.gif|left|200px]]<br /><applet load="1nf2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nf2, resolution 2.20Å" /> | caption="1nf2, resolution 2.20Å" /> | ||
'''X-ray crystal structure of TM0651 from Thermotoga maritima'''<br /> | '''X-ray crystal structure of TM0651 from Thermotoga maritima'''<br /> | ||
==Overview== | ==Overview== | ||
We have determined the crystal structure of a phosphatase with a unique | We have determined the crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima, TM0651 (gi 4981173), at 2.2 A resolution by selenomethionine single-wavelength anomalous diffraction (SAD) techniques. TM0651 is a member of the haloacid dehalogenase (HAD) superfamily, with sequence homology to trehalose-6-phosphate phosphatase and sucrose-6(F)-phosphate phosphohydrolase. Selenomethionine labeled TM0651 crystallized in space group C2 with three monomers per asymmetric unit. Each monomer has approximate dimensions of 65 x 40 x 35 A(3), and contains two domains: a domain of known hydrolase fold characteristic of the HAD family, and a domain with a new tertiary fold consisting of a six-stranded beta-sheet surrounded by four alpha-helices. There is one disulfide bond between residues Cys35 and Cys265 in each monomer. One magnesium ion and one sulfate ion are bound in the active site. The superposition of active site residues with other HAD family members indicates that TM0651 is very likely a phosphatase that acts through the formation of a phosphoaspartate intermediate, which is supported by both NMR titration data and a biochemical assay. Structural and functional database searches and the presence of many aromatic residues in the interface of the two domains suggest the substrate of TM0651 is a carbohydrate molecule. From the crystal structure and NMR data, the protein likely undergoes a conformational change upon substrate binding. | ||
==About this Structure== | ==About this Structure== | ||
1NF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1NF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NF2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: BSGC, Berkeley | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
[[Category: Shin, D | [[Category: Shin, D H.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: thermotoga maritima]] | [[Category: thermotoga maritima]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:26 2008'' | ||
Revision as of 15:05, 21 February 2008
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X-ray crystal structure of TM0651 from Thermotoga maritima
OverviewOverview
We have determined the crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima, TM0651 (gi 4981173), at 2.2 A resolution by selenomethionine single-wavelength anomalous diffraction (SAD) techniques. TM0651 is a member of the haloacid dehalogenase (HAD) superfamily, with sequence homology to trehalose-6-phosphate phosphatase and sucrose-6(F)-phosphate phosphohydrolase. Selenomethionine labeled TM0651 crystallized in space group C2 with three monomers per asymmetric unit. Each monomer has approximate dimensions of 65 x 40 x 35 A(3), and contains two domains: a domain of known hydrolase fold characteristic of the HAD family, and a domain with a new tertiary fold consisting of a six-stranded beta-sheet surrounded by four alpha-helices. There is one disulfide bond between residues Cys35 and Cys265 in each monomer. One magnesium ion and one sulfate ion are bound in the active site. The superposition of active site residues with other HAD family members indicates that TM0651 is very likely a phosphatase that acts through the formation of a phosphoaspartate intermediate, which is supported by both NMR titration data and a biochemical assay. Structural and functional database searches and the presence of many aromatic residues in the interface of the two domains suggest the substrate of TM0651 is a carbohydrate molecule. From the crystal structure and NMR data, the protein likely undergoes a conformational change upon substrate binding.
About this StructureAbout this Structure
1NF2 is a Single protein structure of sequence from Thermotoga maritima with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima., Shin DH, Roberts A, Jancarik J, Yokota H, Kim R, Wemmer DE, Kim SH, Protein Sci. 2003 Jul;12(7):1464-72. PMID:12824492
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