5zjp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae with N-acetylglucosamine-6-phosphate== | ==Structure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae with N-acetylglucosamine-6-phosphate== | ||
<StructureSection load='5zjp' size='340' side='right' caption='[[5zjp]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='5zjp' size='340' side='right'caption='[[5zjp]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zjp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJP OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5zjp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZJP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZJP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=RFW:N-ACETYL-D-GLUCOSAMINE-6-PHOSPHATE'>RFW</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=RFW:N-ACETYL-D-GLUCOSAMINE-6-PHOSPHATE'>RFW</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylglucosamine-6-phosphate_2-epimerase N-acylglucosamine-6-phosphate 2-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.9 5.1.3.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylglucosamine-6-phosphate_2-epimerase N-acylglucosamine-6-phosphate 2-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.9 5.1.3.9] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zjp OCA], [http://pdbe.org/5zjp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zjp RCSB], [http://www.ebi.ac.uk/pdbsum/5zjp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zjp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 23: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: N-acylglucosamine-6-phosphate 2-epimerase]] | [[Category: N-acylglucosamine-6-phosphate 2-epimerase]] | ||
[[Category: Guntupalli, S R]] | [[Category: Guntupalli, S R]] | ||
Revision as of 00:20, 29 October 2020
Structure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae with N-acetylglucosamine-6-phosphateStructure of N-acetylmannosamine-6-phosphate-2-epimerase from Vibrio cholerae with N-acetylglucosamine-6-phosphate
Structural highlights
Function[A0A2K2UT85_VIBCL] Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).[HAMAP-Rule:MF_01235][SAAS:SAAS00761217] Publication Abstract from PubMedSialic acids are nine-carbon sugars that are found abundantly on the cell surfaces of mammals as glycoprotein or glycolipid complexes. Several Gram-negative and Gram-positive bacteria have the ability to scavenge and catabolize sialic acids to use as a carbon source. This gives them an advantage in colonizing sialic acid-rich environments. The genes of the sialic acid catabolic pathway are generally present as the operon nanAKE. The third gene in the operon encodes the enzyme N-acetylmannosamine-6-phosphate 2-epimerase (NanE), which catalyzes the conversion of N-acetylmannosamine 6-phosphate to N-acetylglucosamine 6-phosphate, thus committing it to enter glycolysis. The NanE enzyme belongs to the isomerase class of enzymes possessing the triose phosphate isomerase (TIM) barrel fold. Here, comparative structural and functional characterizations of the NanE epimerases from two pathogenic Gram-negative bacteria, Fusobacterium nucleatum (Fn) and Vibrio cholerae (Vc), have been carried out. Structures of NanE from Vc (VcNanE) with and without ligand bound have been determined to 1.7 and 2.7 A resolution, respectively. The structure of NanE from Fn (FnNanE) has been determined to 2.2 A resolution. The enzymes show kinetic parameters that are consistent with those of Clostridium perfringens NanE. These studies allowed an evaluation of whether NanE may be a good drug target against these pathogenic bacteria. Crystal structures and kinetic analyses of N-acetylmannosamine-6-phosphate 2-epimerases from Fusobacterium nucleatum and Vibrio cholerae.,Manjunath L, Guntupalli SR, Currie MJ, North RA, Dobson RCJ, Nayak V, Subramanian R Acta Crystallogr F Struct Biol Commun. 2018 Jul 1;74(Pt 7):431-440. doi:, 10.1107/S2053230X18008543. Epub 2018 Jun 28. PMID:29969107[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||