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| - | [[Image:1ebb.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ebb| PDB=1ebb | SCENE= }} | | {{STRUCTURE_1ebb| PDB=1ebb | SCENE= }} |
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| - | '''BACILLUS STEAROTHERMOPHILUS YHFR'''
| + | ===BACILLUS STEAROTHERMOPHILUS YHFR=== |
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| - | ==Overview==
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| - | The crystal structure of Bacillus stearothermophilus PhoE (originally termed YhfR), a broad specificity monomeric phosphatase with a molecular mass of approximately 24 kDa, has been solved at 2.3 A resolution in order to investigate its structure and function. PhoE, already identified as a homolog of a cofactor-dependent phosphoglycerate mutase, shares with the latter an alpha/beta/alpha sandwich structure spanning, as a structural excursion, a smaller subdomain composed of two alpha-helices and one short beta-strand. The active site contains residues from both the alpha/beta/alpha sandwich and the sub-domain. With the exception of the hydrophilic catalytic machinery conserved throughout the cofactor-dependent phosphoglycerate mutase family, the active-site cleft is strikingly hydrophobic. Docking studies with two diverse, favored substrates show that 3-phosphoglycerate may bind to the catalytic core, while alpha-napthylphosphate binding also involves the hydrophobic portion of the active-site cleft. Combining a highly favorable phospho group binding site common to these substrate binding modes and data from related enzymes, a catalytic mechanism can be proposed that involves formation of a phosphohistidine intermediate on His10 and likely acid-base behavior of Glu83. Other structural factors contributing to the broad substrate specificity of PhoE can be identified. The dynamic independence of the subdomain may enable the active-site cleft to accommodate substrates of different sizes, although similar motions are present in simulations of cofactor-dependent phosphoglycerate mutases, perhaps favoring a more general functional role. A significant number of entries in protein sequence databases, particularly from unfinished microbial genomes, are more similar to PhoE than to cofactor-dependent phosphoglycerate mutases or to fructose-2,6-bisphosphatases. This PhoE structure will therefore serve as a valuable basis for inference of structural and functional characteristics of these proteins. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11827481}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11827481 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11827481}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Broad specificity phosphatase]] | | [[Category: Broad specificity phosphatase]] |
| | [[Category: Dpgm homolog]] | | [[Category: Dpgm homolog]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:54:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:26:51 2008'' |
Revision as of 21:26, 30 June 2008
Template:STRUCTURE 1ebb
BACILLUS STEAROTHERMOPHILUS YHFR
Template:ABSTRACT PUBMED 11827481
About this Structure
1EBB is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity., Rigden DJ, Mello LV, Setlow P, Jedrzejas MJ, J Mol Biol. 2002 Feb 1;315(5):1129-43. PMID:11827481
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