1ebb
From Proteopedia
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| - | [[Image:1ebb.gif|left|200px]]<br /> | + | [[Image:1ebb.gif|left|200px]]<br /><applet load="1ebb" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ebb" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ebb, resolution 2.3Å" /> | caption="1ebb, resolution 2.3Å" /> | ||
'''BACILLUS STEAROTHERMOPHILUS YHFR'''<br /> | '''BACILLUS STEAROTHERMOPHILUS YHFR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EBB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1EBB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=CAT:Presumed Hydrophobic Substrate Binding Site'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EBB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: broad specificity phosphatase; dpgm homolog]] | [[Category: broad specificity phosphatase; dpgm homolog]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:09:47 2007'' |
Revision as of 13:00, 18 December 2007
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BACILLUS STEAROTHERMOPHILUS YHFR
Overview
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.
About this Structure
1EBB is a Single protein structure of sequence from Geobacillus stearothermophilus with SO4 and GOL as ligands. Known structural/functional Site: . 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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