1m3s
From Proteopedia
(New page: 200px<br /><applet load="1m3s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3s, resolution 1.95Å" /> '''Crystal structure of...) |
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| - | [[Image:1m3s.jpg|left|200px]]<br /><applet load="1m3s" size=" | + | [[Image:1m3s.jpg|left|200px]]<br /><applet load="1m3s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m3s, resolution 1.95Å" /> | caption="1m3s, resolution 1.95Å" /> | ||
'''Crystal structure of YckF from Bacillus subtilis'''<br /> | '''Crystal structure of YckF from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the YckF protein from Bacillus subtilis was | + | The crystal structure of the YckF protein from Bacillus subtilis was determined with MAD phasing and refined at 1.95A resolution. YckF forms a tight tetramer both in crystals and in solution. Conservation of such oligomerization in other phosphate sugar isomerases indicates that the crystallographically observed tetramer is physiologically relevant. The structure of YckF was compared to with its ortholog from Methanococcus jannaschii, MJ1247. Both of these proteins have phosphate hexulose isomerase activity, although neither of the organisms can utilize methane or methanol as source of energy and/or carbon. Extensive sequence and structural similarities with MJ1247 and with the isomerase domain of glucosamine-6-phosphate synthase from Escherichia coli allowed us to group residues contributing to substrate binding or catalysis. Few notable differences among these structures suggest possible cooperativity of the four active sites of the tetramer. Phylogenetic relationships between obligatory and facultative methylotrophs along with B. subtilis and E. coli provide clues about the possible evolution of genes as they loose their physiological importance. |
==About this Structure== | ==About this Structure== | ||
| - | 1M3S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1M3S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Collart, F.]] | [[Category: Collart, F.]] | ||
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
| - | [[Category: Kim, D | + | [[Category: Kim, D E.]] |
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Sanishvili, R.]] | [[Category: Sanishvili, R.]] | ||
[[Category: Wu, R.]] | [[Category: Wu, R.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:09 2008'' |
Revision as of 11:51, 21 February 2008
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Crystal structure of YckF from Bacillus subtilis
Overview
The crystal structure of the YckF protein from Bacillus subtilis was determined with MAD phasing and refined at 1.95A resolution. YckF forms a tight tetramer both in crystals and in solution. Conservation of such oligomerization in other phosphate sugar isomerases indicates that the crystallographically observed tetramer is physiologically relevant. The structure of YckF was compared to with its ortholog from Methanococcus jannaschii, MJ1247. Both of these proteins have phosphate hexulose isomerase activity, although neither of the organisms can utilize methane or methanol as source of energy and/or carbon. Extensive sequence and structural similarities with MJ1247 and with the isomerase domain of glucosamine-6-phosphate synthase from Escherichia coli allowed us to group residues contributing to substrate binding or catalysis. Few notable differences among these structures suggest possible cooperativity of the four active sites of the tetramer. Phylogenetic relationships between obligatory and facultative methylotrophs along with B. subtilis and E. coli provide clues about the possible evolution of genes as they loose their physiological importance.
About this Structure
1M3S is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus subtilis YckF: structural and functional evolution., Sanishvili R, Wu R, Kim DE, Watson JD, Collart F, Joachimiak A, J Struct Biol. 2004 Oct;148(1):98-109. PMID:15363790
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