1f75
From Proteopedia
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|PDB= 1f75 |SIZE=350|CAPTION= <scene name='initialview01'>1f75</scene>, resolution 2.2Å | |PDB= 1f75 |SIZE=350|CAPTION= <scene name='initialview01'>1f75</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Di-trans,poly-cis-decaprenylcistransferase Di-trans,poly-cis-decaprenylcistransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.31 2.5.1.31] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Di-trans,poly-cis-decaprenylcistransferase Di-trans,poly-cis-decaprenylcistransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.31 2.5.1.31] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f75 OCA], [http://www.ebi.ac.uk/pdbsum/1f75 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f75 RCSB]</span> | ||
}} | }} | ||
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[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Zhang, Y W.]] | [[Category: Zhang, Y W.]] | ||
| - | [[Category: SO4]] | ||
[[Category: new fold for isoprenoid synthase]] | [[Category: new fold for isoprenoid synthase]] | ||
[[Category: parallel beta sheet]] | [[Category: parallel beta sheet]] | ||
[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
| - | ''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 20:17:12 2008'' |
Revision as of 17:17, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Di-trans,poly-cis-decaprenylcistransferase, with EC number 2.5.1.31 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26
Overview
Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain elongation onto trans, trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of bacterial cell walls. We report here the crystal structure of UPS as the only three-dimensional structure among cis-prenyl chain elongating enzymes. The structure is classified into a protein fold family and is completely different from the so-called "isoprenoid synthase fold" that is believed to be a common structure for the enzymes relating to isoprenoid biosynthesis. Conserved amino acid residues among cis-prenyl chain elongating enzymes are located around a large hydrophobic cleft in the UPS structure. A structural P-loop motif, which frequently appears in the various kinds of phosphate binding site, is found at the entrance of this cleft. The catalytic site is determined on the basis of these structural features, from which a possible reaction mechanism is proposed.
About this Structure
1F75 is a Single protein structure of sequence from Micrococcus luteus. Full crystallographic information is available from OCA.
Reference
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase., Fujihashi M, Zhang YW, Higuchi Y, Li XY, Koyama T, Miki K, Proc Natl Acad Sci U S A. 2001 Apr 10;98(8):4337-42. Epub 2001 Apr 3. PMID:11287651
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