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[[Image:2zc3.jpg|left|200px]]
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{{STRUCTURE_2zc3|  PDB=2zc3  |  SCENE=  }}
'''Penicillin-binding protein 2X (PBP 2X) acyl-enzyme complex (biapenem) from Streptococcus pneumoniae'''


==Penicillin-binding protein 2X (PBP 2X) acyl-enzyme complex (biapenem) from Streptococcus pneumoniae==
<StructureSection load='2zc3' size='340' side='right'caption='[[2zc3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2zc3]] is a 6 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=2ZC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZC3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMG:(4R,5S)-3-(6,7-DIHYDRO-5H-PYRAZOLO[1,2-A][1,2,4]TRIAZOL-4-IUM-6-YLSULFANYL)-5-[(1S,2R)-1-FORMYL-2-HYDROXYPROPYL]-4-METHYL-4,5-DIHYDRO-1H-PYRROLE-2-CARBOXYLATE'>BMG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2zc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zc3 OCA], [https://pdbe.org/2zc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zc3 RCSB], [https://www.ebi.ac.uk/pdbsum/2zc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zc3 ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zc/2zc3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zc3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Biapenem is a parenteral carbapenem antibiotic that exhibits wide-ranging antibacterial activity, remarkable chemical stability, and extensive stability against human renal dehydropeptidase-I. Tebipenem is the active form of tebipenem pivoxil, a novel oral carbapenem antibiotic that has a high level of bioavailability in humans, in addition to the above-mentioned features. beta-lactam antibiotics, including carbapenems, target penicillin-binding proteins (PBPs), which are membrane-associated enzymes that play essential roles in peptidoglycan biosynthesis. To envisage the binding of carbapenems to PBPs, we determined the crystal structures of the trypsin-digested forms of both PBP 2X and PBP 1A from Streptococcus pneumoniae strain R6, each complexed with biapenem or tebipenem. The structures of the complexes revealed that the carbapenem C-2 side chains form hydrophobic interactions with Trp374 and Thr526 of PBP 2X and with Trp411 and Thr543 of PBP 1A. The Trp and Thr residues are conserved in PBP 2B. These results suggest that interactions between the C-2 side chains of carbapenems and the conserved Trp and Thr residues in PBPs play important roles in the binding of carbapenems to PBPs.


==Overview==
Crystal structures of biapenem and tebipenem complexed with penicillin-binding proteins 2X and 1A from Streptococcus pneumoniae.,Yamada M, Watanabe T, Baba N, Takeuchi Y, Ohsawa F, Gomi S Antimicrob Agents Chemother. 2008 Jun;52(6):2053-60. Epub 2008 Apr 7. PMID:18391040<ref>PMID:18391040</ref>
Biapenem is a parenteral carbapenem antibiotic that exhibits wide-ranging antibacterial activity, remarkable chemical stability, and extensive stability against human renal dehydropeptidase-I. Tebipenem is the active form of tebipenem pivoxil, a novel oral carbapenem antibiotic that has a high level of bioavailability in humans, in addition to the above-mentioned features. beta-lactam antibiotics, including carbapenems, target penicillin-binding proteins (PBPs), which are membrane-associated enzymes that play essential roles in peptidoglycan biosynthesis. To envisage the binding of carbapenems to PBPs, we determined the crystal structures of the trypsin-digested forms of both PBP 2X and PBP 1A from Streptococcus pneumoniae strain R6, each complexed with biapenem or tebipenem. The structures of the complexes revealed that the carbapenem C-2 side chains form hydrophobic interactions with Trp374 and Thr526 of PBP 2X and with Trp411 and Thr543 of PBP 1A. The Trp and Thr residues are conserved in PBP 2B. These results suggest that interactions between the C-2 side chains of carbapenems and the conserved Trp and Thr residues in PBPs play important roles in the binding of carbapenems to PBPs.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ZC3 is a [[Protein complex]] structure of sequences 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=2ZC3 OCA].
</div>
<div class="pdbe-citations 2zc3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structures of biapenem and tebipenem complexed with penicillin-binding proteins 2X and 1A from Streptococcus pneumoniae., Yamada M, Watanabe T, Baba N, Takeuchi Y, Ohsawa F, Gomi S, Antimicrob Agents Chemother. 2008 Jun;52(6):2053-60. Epub 2008 Apr 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18391040 18391040]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
[[Category: Takeuchi, Y.]]
[[Category: Takeuchi Y]]
[[Category: Watanabe, T.]]
[[Category: Watanabe T]]
[[Category: Yamada, M.]]
[[Category: Yamada M]]
[[Category: Antibiotic resistance]]
[[Category: Antibiotic]]
[[Category: Biapenem]]
[[Category: Biosynthetic protein]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Cell shape]]
[[Category: Cell wall]]
[[Category: Cell wall biogenesis/degradation]]
[[Category: Membrane]]
[[Category: Penicillin-binding]]
[[Category: Peptidoglycan synthesis]]
[[Category: Secreted]]
[[Category: Transmembrane]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 10:01:03 2008''

Latest revision as of 05:38, 17 October 2024

Penicillin-binding protein 2X (PBP 2X) acyl-enzyme complex (biapenem) from Streptococcus pneumoniae

2zc3, resolution 2.50Å

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