1iho
From Proteopedia
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|PDB= 1iho |SIZE=350|CAPTION= <scene name='initialview01'>1iho</scene>, resolution 1.70Å | |PDB= 1iho |SIZE=350|CAPTION= <scene name='initialview01'>1iho</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Pantoate--beta-alanine_ligase Pantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.1 6.3.2.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantoate--beta-alanine_ligase Pantoate--beta-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.1 6.3.2.1] </span> |
|GENE= panc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= panc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iho OCA], [http://www.ebi.ac.uk/pdbsum/1iho PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iho RCSB]</span> | ||
}} | }} | ||
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[[Category: Lewendon, A.]] | [[Category: Lewendon, A.]] | ||
[[Category: Smith, A.]] | [[Category: Smith, A.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: TRS]] | ||
[[Category: apo]] | [[Category: apo]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
| - | ''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 21:19:55 2008'' |
Revision as of 18:19, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | panc (Escherichia coli) | ||||||
| Activity: | Pantoate--beta-alanine ligase, with EC number 6.3.2.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI
Overview
BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction. RESULTS: We describe the overexpression, purification, and crystal structure of recombinant pantothenate synthetase from E. coli. The structure was solved by a selenomethionine multiwavelength anomalous dispersion experiment and refined against native data to a final R(cryst) of 22.6% (R(free) = 24.9%) at 1.7 A resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a Rossmann fold, contains the active site cavity, with the C-terminal domain forming a hinged lid. CONCLUSIONS: The N-terminal domain is structurally very similar to class I aminoacyl-tRNA synthetases and is thus a member of the cytidylyltransferase superfamily. This relationship has been used to suggest the location of the ATP and pantoate binding sites and the nature of hinge bending that leads to the ternary enzyme-pantoate-ATP complex.
About this Structure
1IHO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily., von Delft F, Lewendon A, Dhanaraj V, Blundell TL, Abell C, Smith AG, Structure. 2001 May 9;9(5):439-50. PMID:11377204
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