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6cb2

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Revision as of 06:20, 6 June 2018

Crystal structure of Escherichia coli UppP

Structural highlights

6cb2 is a 1 chain structure with sequence from Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	uppP, bacA, upk, b3057, JW3029 (ECO57)
Activity:	Undecaprenyl-diphosphate phosphatase, with EC number 3.6.1.27
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UPPP_ECOLI] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.^[1]

Publication Abstract from PubMed

Undecaprenyl pyrophosphate phosphatase (UppP) is an integral membrane protein that recycles the lipid carrier essential to the ongoing biosynthesis of the bacterial cell wall. Individual building blocks of peptidoglycan are assembled in the cytoplasm on undecaprenyl phosphate (C55-P) before being flipped to the periplasmic face, where they are polymerized and transferred to the existing cell wall sacculus, resulting in the side product undecaprenyl pyrophosphate (C55-PP). Interruption of UppP's regeneration of C55-P from C55-PP leads to the buildup of cell wall intermediates and cell lysis. We present the crystal structure of UppP from Escherichia coli at 2.0 A resolution, which reveals the mechanistic basis for intramembranal phosphatase action and substrate specificity using an inverted topology repeat. In addition, the observation of key structural motifs common to a variety of cross membrane transporters hints at a potential flippase function in the specific relocalization of the C55-P product back to the cytosolic space.

Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling.,Workman SD, Worrall LJ, Strynadka NCJ Nat Commun. 2018 Mar 20;9(1):1159. doi: 10.1038/s41467-018-03547-8. PMID:29559664^[2]

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

References

↑ El Ghachi M, Derbise A, Bouhss A, Mengin-Lecreulx D. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J Biol Chem. 2005 May 13;280(19):18689-95. Epub 2005 Mar 18. PMID:15778224 doi:http://dx.doi.org/M412277200
↑ Workman SD, Worrall LJ, Strynadka NCJ. Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling. Nat Commun. 2018 Mar 20;9(1):1159. doi: 10.1038/s41467-018-03547-8. PMID:29559664 doi:http://dx.doi.org/10.1038/s41467-018-03547-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6cb2"

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[6cb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CB2 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uppP, bacA, upk, Z4410, ECs3940 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uppP, bacA, upk, b3057, JW3029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Undecaprenyl-diphosphate_phosphatase Undecaprenyl-diphosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.27 3.6.1.27] </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=6cb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cb2 OCA], [http://pdbe.org/6cb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cb2 RCSB], [http://www.ebi.ac.uk/pdbsum/6cb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cb2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UPPP_ECO57 UPPP_ECO57]] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
+[[http://www.uniprot.org/uniprot/UPPP_ECOLI UPPP_ECOLI]] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.<ref>PMID:15778224</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

6cb2

From Proteopedia

Revision as of 06:20, 6 June 2018

Crystal structure of Escherichia coli UppP

Structural highlights

Function

Publication Abstract from PubMed

References

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