4j6e: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== | ==Structure of LPXI D225A Mutant== | ||
[[4j6e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <StructureSection load='4j6e' size='340' side='right' caption='[[4j6e]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
[[ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j6e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caucn Caucn]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ggi 4ggi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J6E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UDG:(2R,3R,4R,5S,6R)-2-{[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-5-HYDROXY-6-(HYDROXYMETHYL)-3-{[(3R)-3-HYDROXYTETRADECANOYL]AMINO}TETRAHYDRO-2H-PYRAN-4-YL+(3R)-3-HYDROXYTETRADECANOATE'>UDG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ggm|4ggm]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">77330127, CCNA_01987, CC_1910, lpxI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565050 CAUCN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-2,3-diacylglucosamine_diphosphatase UDP-2,3-diacylglucosamine diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.54 3.6.1.54] </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=4j6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j6e OCA], [http://pdbe.org/4j6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j6e RCSB], [http://www.ebi.ac.uk/pdbsum/4j6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j6e ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes in lipid metabolism acquire and deliver hydrophobic substrates and products from within lipid bilayers. The structure at 2.55 A of one isozyme of a constitutive enzyme in lipid A biosynthesis, LpxI from Caulobacter crescentus, has a novel fold. Two domains close around a completely sequestered substrate, UDP-2,3-diacylglucosamine, and open to release products either to the neighboring enzyme in a putative multienzyme complex or to the bilayer. Mutation analysis identifies Asp225 as key to Mg(2+)-catalyzed diphosphate hydrolysis. These structures provide snapshots of the enzymatic synthesis of a critical lipid A precursor. | |||
LpxI structures reveal how a lipid A precursor is synthesized.,Metzger LE 4th, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM Nat Struct Mol Biol. 2012 Nov;19(11):1132-8. doi: 10.1038/nsmb.2393. Epub 2012, Oct 7. PMID:23042606<ref>PMID:23042606</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4j6e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caucn]] | |||
[[Category: UDP-2,3-diacylglucosamine diphosphatase]] | [[Category: UDP-2,3-diacylglucosamine diphosphatase]] | ||
[[Category: CSMP, Center for Structures of Membrane Proteins | [[Category: CSMP, Center for Structures of Membrane Proteins]] | ||
[[Category: Finer-Moore, J S | [[Category: Finer-Moore, J S]] | ||
[[Category: IV, L E.Metzger | [[Category: IV, L E.Metzger]] | ||
[[Category: Lee, J K | [[Category: Lee, J K]] | ||
[[Category: Raetz, C R.H | [[Category: Raetz, C R.H]] | ||
[[Category: Stroud, R M | [[Category: Stroud, R M]] | ||
[[Category: Center for structures of membrane protein]] | [[Category: Center for structures of membrane protein]] | ||
[[Category: Csmp]] | [[Category: Csmp]] | ||
Revision as of 11:42, 4 August 2016
Structure of LPXI D225A MutantStructure of LPXI D225A Mutant
Structural highlights
Publication Abstract from PubMedEnzymes in lipid metabolism acquire and deliver hydrophobic substrates and products from within lipid bilayers. The structure at 2.55 A of one isozyme of a constitutive enzyme in lipid A biosynthesis, LpxI from Caulobacter crescentus, has a novel fold. Two domains close around a completely sequestered substrate, UDP-2,3-diacylglucosamine, and open to release products either to the neighboring enzyme in a putative multienzyme complex or to the bilayer. Mutation analysis identifies Asp225 as key to Mg(2+)-catalyzed diphosphate hydrolysis. These structures provide snapshots of the enzymatic synthesis of a critical lipid A precursor. LpxI structures reveal how a lipid A precursor is synthesized.,Metzger LE 4th, Lee JK, Finer-Moore JS, Raetz CR, Stroud RM Nat Struct Mol Biol. 2012 Nov;19(11):1132-8. doi: 10.1038/nsmb.2393. Epub 2012, Oct 7. PMID:23042606[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||||