1f75
From Proteopedia
(New page: 200px<br /><applet load="1f75" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f75, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1f75.gif|left|200px]]<br /><applet load="1f75" size=" | + | [[Image:1f75.gif|left|200px]]<br /><applet load="1f75" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f75, resolution 2.2Å" /> | caption="1f75, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26'''<br /> | '''CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain | + | 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== | ==About this Structure== | ||
| - | 1F75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1F75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Micrococcus_luteus Micrococcus luteus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F75 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Higuchi, Y.]] | [[Category: Higuchi, Y.]] | ||
[[Category: Koyama, T.]] | [[Category: Koyama, T.]] | ||
| - | [[Category: Li, X | + | [[Category: Li, X Y.]] |
[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
| - | [[Category: Zhang, Y | + | [[Category: Zhang, Y W.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: new fold for isoprenoid synthase]] | [[Category: new fold for isoprenoid synthase]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:48 2008'' |
Revision as of 10:35, 21 February 2008
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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 with as ligand. Active as Di-trans,poly-cis-decaprenylcistransferase, with EC number 2.5.1.31 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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