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5hla

From Proteopedia

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Current revision

E. coli PBP1b in complex with acyl-cephalexin and moenomycin

Structural highlights

5hla is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.36Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PBPB_ECOLI Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).

Publication Abstract from PubMed

In Escherichia coli, the peptidoglycan cell wall is synthesized by bifunctional penicillin-binding proteins such as PBP1b that have both transpeptidase and transglycosylase activities. The PBP1b transpeptidase domain is a major target of beta-lactams and therefore it is important to attain a detailed understanding of its inhibition. The peptidoglycan glycosyltransferase domain of PBP1b is also considered an excellent antibiotic target, yet is not exploited by any clinically approved antibacterials. Herein, we adapt a pyrophosphate sensor assay to monitor PBP1b catalyzed glycosyltransfer and present an improved crystallographic model for inhibition of the PBP1b glycosyltransferase domain by the potent substrate analogue moenomycin. We elucidate the structure of a previously disordered region in the glycosyltransferase active site and discuss its implications with regards to peptidoglycan polymerization. Furthermore, we solve the crystal structures of E. coli PBP1b bound to multiple different beta-lactams in the transpeptidase active site, and complement this data with gel based competition assays to provide a detailed structural understanding of its inhibition. Taken together, this biochemical and structural data allows us to propose new insights into inhibition of both enzymatic domains in PBP1b.

Escherichia coli Penicillin-Binding Protein 1B: Structural Insights into Inhibition.,King DT, Wasney GA, Nosella M, Fong A, Strynadka NC J Biol Chem. 2016 Nov 29. pii: jbc.M116.718403. PMID:27899450^[1]

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

References

↑ King DT, Wasney GA, Nosella M, Fong A, Strynadka NC. Escherichia coli Penicillin-Binding Protein 1B: Structural Insights into Inhibition. J Biol Chem. 2016 Nov 29. pii: jbc.M116.718403. PMID:27899450 doi:http://dx.doi.org/10.1074/jbc.M116.718403

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/5hla"

Categories: Escherichia coli K-12 | Large Structures | King DT | Strynadka NCJ

@@ Line 3: / Line 3: @@
 <StructureSection load='5hla' size='340' side='right'caption='[[5hla]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hla]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HLA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hla]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HLA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=63U:(2S)-2-[(1R)-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5-METHYL-3,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>63U</scene>, <scene name='pdbligand=M0E:MOENOMYCIN'>M0E</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]] 2.36&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hl9|5hl9]], [[5hlb|5hlb]], [[5hld|5hld]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=63U:(2S)-2-[(1R)-1-{[(2R)-2-AMINO-2-PHENYLACETYL]AMINO}-2-OXOETHYL]-5-METHYL-3,6-DIHYDRO-2H-1,3-THIAZINE-4-CARBOXYLIC+ACID'>63U</scene>, <scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mrcB, pbpF, ponB, b0149, JW0145 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5hla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hla OCA], [https://pdbe.org/5hla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hla RCSB], [https://www.ebi.ac.uk/pdbsum/5hla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hla ProSAT]</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=5hla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hla OCA], [http://pdbe.org/5hla PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hla RCSB], [http://www.ebi.ac.uk/pdbsum/5hla PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hla ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PBPB_ECOLI PBPB_ECOLI]] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
+[https://www.uniprot.org/uniprot/PBPB_ECOLI PBPB_ECOLI] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: King, D T]]
+[[Category: King DT]]
-[[Category: Strynadka, N C.J]]
+[[Category: Strynadka NCJ]]
-[[Category: Inhibitor complex]]
-[[Category: Penicillin-binding protein]]
-[[Category: Transferase-transferase inhibitor complex]]
-[[Category: Transglycosylase]]
-[[Category: Transpeptidase]]

5hla

From Proteopedia

Current revision

E. coli PBP1b in complex with acyl-cephalexin and moenomycin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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