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1pmd

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Revision as of 09:31, 8 September 2021

PENICILLIN-BINDING PROTEIN 2X (PBP-2X)

Structural highlights

1pmd is a 1 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PBPX_STRPN] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.

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

All beta-lactam antibiotics exert their biological effects by interacting with a unique class of proteins, the penicillin-binding proteins (PBPs). These membrane proteins are involved in the biosynthesis of the murein or peptidoglycan, a mesh-like structure which completely surrounds the bacterial cell. Sequence similarities indicate that one domain of these proteins belongs to a large family of beta-lactam-recognizing proteins, which includes the active-site serine beta-lactamases. We here report the first three-dimensional crystal structure of a high molecular weight penicillin-binding protein, PBP2x of Streptococcus pneumoniae, at 3.5 A resolution. The molecule has three domains, the central domain being a transpeptidase, which is a suitable target for antibiotic development.

X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme.,Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631^[1]

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

References

↑ Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat Struct Biol. 1996 Mar;3(3):284-9. PMID:8605631

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pmd"

@@ Line 3: / Line 3: @@
 <StructureSection load='1pmd' size='340' side='right'caption='[[1pmd]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pmd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PMD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pmd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMD FirstGlance]. <br>
-</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=1pmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmd OCA], [http://pdbe.org/1pmd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pmd RCSB], [http://www.ebi.ac.uk/pdbsum/1pmd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmd ProSAT]</span></td></tr>
+</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=1pmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmd OCA], [https://pdbe.org/1pmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmd RCSB], [https://www.ebi.ac.uk/pdbsum/1pmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PBPX_STRPN PBPX_STRPN]] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.
+[[https://www.uniprot.org/uniprot/PBPX_STRPN PBPX_STRPN]] Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1pmd

From Proteopedia

Revision as of 09:31, 8 September 2021

PENICILLIN-BINDING PROTEIN 2X (PBP-2X)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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