5kh4

From Proteopedia

(Difference between revisions)

Revision as of 10:46, 27 September 2023

Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS) with FARNESYL DIPHOSPHATE

Structural highlights

5kh4 is a 2 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ISPT_STRPN Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.

Publication Abstract from PubMed

Undecaprenyl pyrophosphate synthase (UppS) is an essential enzyme in bacterial cell wall synthesis. Here we report the discovery of Staphylococcus aureus UppS inhibitors from an Encoded Library Technology screen and demonstrate binding to the hydrophobic substrate site through cocrystallography studies. The use of bacterial strains with regulated uppS expression and inhibitor resistant mutant studies confirmed that the whole cell activity was the result of UppS inhibition, validating UppS as a druggable antibacterial target.

Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase.,Concha N, Huang J, Bai X, Benowitz A, Brady P, Grady LC, Kryn LH, Holmes D, Ingraham K, Jin Q, Pothier Kaushansky L, McCloskey L, Messer JA, O'Keefe H, Patel A, Satz AL, Sinnamon RH, Schneck J, Skinner SR, Summerfield J, Taylor A, Taylor JD, Evindar G, Stavenger RA J Med Chem. 2016 Jul 20. PMID:27379833^[1]

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

References

↑ Concha N, Huang J, Bai X, Benowitz A, Brady P, Grady LC, Kryn LH, Holmes D, Ingraham K, Jin Q, Pothier Kaushansky L, McCloskey L, Messer JA, O'Keefe H, Patel A, Satz AL, Sinnamon RH, Schneck J, Skinner SR, Summerfield J, Taylor A, Taylor JD, Evindar G, Stavenger RA. Discovery and Characterization of a Class of Pyrazole Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase. J Med Chem. 2016 Jul 20. PMID:27379833 doi:http://dx.doi.org/10.1021/acs.jmedchem.6b00746

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kh4"

Categories: Large Structures | Streptococcus pneumoniae TIGR4 | Concha NO

@@ Line 3: / Line 3: @@
 <StructureSection load='5kh4' size='340' side='right'caption='[[5kh4]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5kh4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KH4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KH4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5kh4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KH4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uppS, SP_0261 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh4 OCA], [http://pdbe.org/5kh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kh4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh4 ProSAT]</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=5kh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh4 OCA], [https://pdbe.org/5kh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kh4 RCSB], [https://www.ebi.ac.uk/pdbsum/5kh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ISPT_STRPN ISPT_STRPN]] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
+[https://www.uniprot.org/uniprot/ISPT_STRPN ISPT_STRPN] Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Strpn]]
+[[Category: Streptococcus pneumoniae TIGR4]]
-[[Category: Concha, N O]]
+[[Category: Concha NO]]
-[[Category: Bacterial]]
-[[Category: Native]]
-[[Category: Transferase]]
-[[Category: Undecaprenyl s. pneumoniae]]
-[[Category: Upp]]

5kh4

From Proteopedia

Revision as of 10:46, 27 September 2023

Crystal Structure of Steptococcus pneumoniae Undecaprenyl pyrophosphate Synthase (UPPS) with FARNESYL DIPHOSPHATE

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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