1ep0
From Proteopedia
(New page: 200px<br /><applet load="1ep0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ep0, resolution 1.50Å" /> '''HIGH RESOLUTION CRYS...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ep0.gif|left|200px]]<br /><applet load="1ep0" size=" | + | [[Image:1ep0.gif|left|200px]]<br /><applet load="1ep0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ep0, resolution 1.50Å" /> | caption="1ep0, resolution 1.50Å" /> | ||
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | '''HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase | + | Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase (RmlC) is involved in the biosynthesis of dTDP-l-rhamnose, which is an essential component of the bacterial cell wall. The crystal structure of RmlC from Methanobacterium thermoautotrophicum was determined in the presence and absence of dTDP, a substrate analogue. RmlC is a homodimer comprising a central jelly roll motif, which extends in two directions into longer beta-sheets. Binding of dTDP is stabilized by ionic interactions to the phosphate group and by a combination of ionic and hydrophobic interactions with the base. The active site, which is located in the center of the jelly roll, is formed by residues that are conserved in all known RmlC sequence homologues. The conservation of the active site residues suggests that the mechanism of action is also conserved and that the RmlC structure may be useful in guiding the design of antibacterial drugs. |
==About this Structure== | ==About this Structure== | ||
| - | 1EP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] Full crystallographic information is available from [http:// | + | 1EP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP0 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: dTDP-4-dehydrorhamnose 3,5-epimerase]] | [[Category: dTDP-4-dehydrorhamnose 3,5-epimerase]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
[[Category: Bochkarev, A.]] | [[Category: Bochkarev, A.]] | ||
[[Category: Christendat, D.]] | [[Category: Christendat, D.]] | ||
| - | [[Category: Edwards, A | + | [[Category: Edwards, A M.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
| - | [[Category: Pai, E | + | [[Category: Pai, E F.]] |
[[Category: Saridakis, V.]] | [[Category: Saridakis, V.]] | ||
[[Category: dtdp-4-dehydrorhamnose epimerase]] | [[Category: dtdp-4-dehydrorhamnose epimerase]] | ||
| Line 29: | Line 29: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:07 2008'' |
Revision as of 10:30, 21 February 2008
|
HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
Overview
Deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-d-hexulose 3, 5-epimerase (RmlC) is involved in the biosynthesis of dTDP-l-rhamnose, which is an essential component of the bacterial cell wall. The crystal structure of RmlC from Methanobacterium thermoautotrophicum was determined in the presence and absence of dTDP, a substrate analogue. RmlC is a homodimer comprising a central jelly roll motif, which extends in two directions into longer beta-sheets. Binding of dTDP is stabilized by ionic interactions to the phosphate group and by a combination of ionic and hydrophobic interactions with the base. The active site, which is located in the center of the jelly roll, is formed by residues that are conserved in all known RmlC sequence homologues. The conservation of the active site residues suggests that the mechanism of action is also conserved and that the RmlC structure may be useful in guiding the design of antibacterial drugs.
About this Structure
1EP0 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Active as dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13 Full crystallographic information is available from OCA.
Reference
Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP., Christendat D, Saridakis V, Dharamsi A, Bochkarev A, Pai EF, Arrowsmith CH, Edwards AM, J Biol Chem. 2000 Aug 11;275(32):24608-12. PMID:10827167
Page seeded by OCA on Thu Feb 21 12:30:07 2008
Categories: Methanothermobacter thermautotrophicus | Single protein | DTDP-4-dehydrorhamnose 3,5-epimerase | Arrowsmith, C H. | Bochkarev, A. | Christendat, D. | Edwards, A M. | NESG, Northeast Structural Genomics Consortium. | Pai, E F. | Saridakis, V. | Dtdp-4-dehydrorhamnose epimerase | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Racemase | Structural genomics
