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2uwx

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Revision as of 11:12, 17 June 2020

Active site restructuring regulates ligand recognition in class A penicillin-binding proteins

Structural highlights

2uwx is a 1 chain structure with sequence from Strr6. This structure supersedes the now removed PDB entry 2bg3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	2uwy
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial cell division is a complex, multimolecular process that requires biosynthesis of new peptidoglycan by penicillin-binding proteins (PBPs) during cell wall elongation and septum formation steps. Streptococcus pneumoniae has three bifunctional (class A) PBPs that catalyze both polymerization of glycan chains (glycosyltransfer) and cross-linking of pentapeptidic bridges (transpeptidation) during the peptidoglycan biosynthetic process. In addition to playing important roles in cell division, PBPs are also the targets for beta-lactam antibiotics and thus play key roles in drug-resistance mechanisms. The crystal structure of a soluble form of pneumococcal PBP1b (PBP1b*) has been solved to 1.9 A, thus providing previously undescribed structural information regarding a class A PBP from any organism. PBP1b* is a three-domain molecule harboring a short peptide from the glycosyltransferase domain bound to an interdomain linker region, the transpeptidase domain, and a C-terminal region. The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft. The open and closed structures of PBP1b* suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process. In addition, this structure provides an initial framework for the understanding of the role of class A PBPs in the development of antibiotic resistance.

Active site restructuring regulates ligand recognition in class A penicillin-binding proteins.,Macheboeuf P, Di Guilmi AM, Job V, Vernet T, Dideberg O, Dessen A Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):577-82. Epub 2005 Jan 6. PMID:15637155^[1]

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

References

↑ Macheboeuf P, Di Guilmi AM, Job V, Vernet T, Dideberg O, Dessen A. Active site restructuring regulates ligand recognition in class A penicillin-binding proteins. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):577-82. Epub 2005 Jan 6. PMID:15637155

1 Structural highlights
2 Evolutionary Conservation
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/2uwx"

@@ Line 1: / Line 1: @@
 ==Active site restructuring regulates ligand recognition in class A penicillin-binding proteins==
-<StructureSection load='2uwx' size='340' side='right' caption='[[2uwx]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
+<StructureSection load='2uwx' size='340' side='right'caption='[[2uwx]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2uwx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bg3 2bg3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2UWX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2uwx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bg3 2bg3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UWX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2UWX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NC1:NITROCEFIN+ACYL-SERINE'>NC1</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2uwy|2uwy]]</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=2uwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwx OCA], [http://pdbe.org/2uwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uwx RCSB], [http://www.ebi.ac.uk/pdbsum/2uwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwx ProSAT]</span></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=2uwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uwx OCA], [http://pdbe.org/2uwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2uwx RCSB], [http://www.ebi.ac.uk/pdbsum/2uwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2uwx ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Penicillin-binding protein|Penicillin-binding protein]]
+*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Strr6]]
 [[Category: Dessen, A]]

2uwx

From Proteopedia

Revision as of 11:12, 17 June 2020

Active site restructuring regulates ligand recognition in class A penicillin-binding proteins

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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