1ebb
From Proteopedia
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|PDB= 1ebb |SIZE=350|CAPTION= <scene name='initialview01'>1ebb</scene>, resolution 2.3Å | |PDB= 1ebb |SIZE=350|CAPTION= <scene name='initialview01'>1ebb</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=CAT:Presumed+Hydrophobic+Substrate+Binding+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Presumed+Hydrophobic+Substrate+Binding+Site'>CAT</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebb OCA], [http://www.ebi.ac.uk/pdbsum/1ebb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ebb RCSB]</span> | ||
}} | }} | ||
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[[Category: Jedrzejas, M J.]] | [[Category: Jedrzejas, M J.]] | ||
[[Category: Rigden, D J.]] | [[Category: Rigden, D J.]] | ||
| - | [[Category: | + | [[Category: broad specificity phosphatase]] |
| - | [[Category: | + | [[Category: dpgm homolog]] |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:12 2008'' |
Revision as of 16:59, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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