2fuk
From Proteopedia
(New page: 200px<br /><applet load="2fuk" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fuk, resolution 1.6Å" /> '''Crystal structure of ...) |
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==Overview== | ==Overview== | ||
| - | XC6422 is a conserved hypothetical protein from Xanthomonas campestris | + | XC6422 is a conserved hypothetical protein from Xanthomonas campestris pathovar campestris (Xcc), a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. The protein consists of 220 amino acids and its structure has been determined to 1.6 A resolution using the multi-wavelength anomalous dispersion (MAD) method. Although it has very low sequence identity to protein sequences in the PDB (less than 20%), the determined structure nevertheless shows that it belongs to the superfamily of serine alpha/beta-hydrolases, with an active site that is fully accessible to solvent owing to the absence of a lid domain. Modelling studies with the serine esterase inhibitor E600 indicate that XC6422 adopts a conserved Ser-His-Asp catalytic triad common to this superfamily and has a preformed oxyanion hole for catalytic activation. These structural features suggest that XC6422 is most likely to be a hydrolase active on a soluble ester or a small lipid. An extra strand preceding the first beta-strand in the canonical alpha/beta-hydrolase fold leads to extensive subunit interactions between XC6422 monomers, which may explain why XC6422 crystals of good diffraction quality can grow to dimensions of up to 1.5 mm in a few days. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase., Yang CY, Chin KH, Chou CC, Wang AH, Chou SH, Acta | + | Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase., Yang CY, Chin KH, Chou CC, Wang AH, Chou SH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):498-503. Epub 2006 May 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16754966 16754966] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xanthomonas campestris]] | [[Category: Xanthomonas campestris]] | ||
| - | [[Category: Chin, K | + | [[Category: Chin, K H.]] |
| - | [[Category: Chou, C | + | [[Category: Chou, C C.]] |
| - | [[Category: Chou, S | + | [[Category: Chou, S H.]] |
| - | [[Category: Wang, A | + | [[Category: Wang, A H.J.]] |
| - | [[Category: Yang, C | + | [[Category: Yang, C Y.]] |
[[Category: a/b hydrolase]] | [[Category: a/b hydrolase]] | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| Line 23: | Line 23: | ||
[[Category: xanthomonas campestris]] | [[Category: xanthomonas campestris]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:26 2008'' |
Revision as of 15:25, 21 February 2008
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Crystal structure of XC6422 from Xanthomonas campestris: a member of a/b serine hydrolase without lid at 1.6 resolution
Overview
XC6422 is a conserved hypothetical protein from Xanthomonas campestris pathovar campestris (Xcc), a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. The protein consists of 220 amino acids and its structure has been determined to 1.6 A resolution using the multi-wavelength anomalous dispersion (MAD) method. Although it has very low sequence identity to protein sequences in the PDB (less than 20%), the determined structure nevertheless shows that it belongs to the superfamily of serine alpha/beta-hydrolases, with an active site that is fully accessible to solvent owing to the absence of a lid domain. Modelling studies with the serine esterase inhibitor E600 indicate that XC6422 adopts a conserved Ser-His-Asp catalytic triad common to this superfamily and has a preformed oxyanion hole for catalytic activation. These structural features suggest that XC6422 is most likely to be a hydrolase active on a soluble ester or a small lipid. An extra strand preceding the first beta-strand in the canonical alpha/beta-hydrolase fold leads to extensive subunit interactions between XC6422 monomers, which may explain why XC6422 crystals of good diffraction quality can grow to dimensions of up to 1.5 mm in a few days.
About this Structure
2FUK is a Protein complex structure of sequences from Xanthomonas campestris. Full crystallographic information is available from OCA.
Reference
Structure of XC6422 from Xanthomonas campestris at 1.6 A resolution: a small serine alpha/beta-hydrolase., Yang CY, Chin KH, Chou CC, Wang AH, Chou SH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):498-503. Epub 2006 May 31. PMID:16754966
Page seeded by OCA on Thu Feb 21 17:25:26 2008
