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1ep0

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Revision as of 06:32, 11 August 2021

HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Structural highlights

1ep0 is a 1 chain structure with sequence from "methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1epz
Activity:	dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[RMLC_METTH] Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Christendat D, Saridakis V, Dharamsi A, Bochkarev A, Pai EF, Arrowsmith CH, Edwards AM. Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP. J Biol Chem. 2000 Aug 11;275(32):24608-12. PMID:10827167 doi:10.1074/jbc.C000238200
↑ Christendat D, Saridakis V, Dharamsi A, Bochkarev A, Pai EF, Arrowsmith CH, Edwards AM. Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP. J Biol Chem. 2000 Aug 11;275(32):24608-12. PMID:10827167 doi:10.1074/jbc.C000238200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ep0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ep0' size='340' side='right'caption='[[1ep0]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ep0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EP0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ep0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EP0 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1epz|1epz]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1epz|1epz]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ep0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ep0 OCA], [http://pdbe.org/1ep0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ep0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ep0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ep0 ProSAT], [http://www.topsan.org/Proteins/NESGC/1ep0 TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ep0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ep0 OCA], [https://pdbe.org/1ep0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ep0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ep0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ep0 ProSAT], [https://www.topsan.org/Proteins/NESGC/1ep0 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RMLC_METTH RMLC_METTH]] Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.<ref>PMID:10827167</ref>
+[[https://www.uniprot.org/uniprot/RMLC_METTH RMLC_METTH]] Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.<ref>PMID:10827167</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ep0

From Proteopedia

Revision as of 06:32, 11 August 2021

HIGH RESOLUTION CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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