3fwl: Difference between revisions

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-[[Image:3fwl.png|left|200px]]
-{{STRUCTURE_3fwl|  PDB=3fwl  |  SCENE=  }}
+==Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli==
+<StructureSection load='3fwl' size='340' side='right'caption='[[3fwl]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3fwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FWL 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]] 3.086&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fwl OCA], [https://pdbe.org/3fwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fwl RCSB], [https://www.ebi.ac.uk/pdbsum/3fwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fwl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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).
+== 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/fw/3fwl_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=3fwl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Drug-resistant bacteria have caused serious medical problems in recent years, and the need for new antibacterial agents is undisputed. Transglycosylase, a multidomain membrane protein essential for cell wall synthesis, is an excellent target for the development of new antibiotics. Here, we determined the X-ray crystal structure of the bifunctional transglycosylase penicillin-binding protein 1b (PBP1b) from Escherichia coli in complex with its inhibitor moenomycin to 2.16-A resolution. In addition to the transglycosylase and transpeptidase domains, our structure provides a complete visualization of this important antibacterial target, and reveals a domain for protein-protein interaction and a transmembrane helix domain essential for substrate binding, enzymatic activity, and membrane orientation.
-===Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli===
+Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.,Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C Proc Natl Acad Sci U S A. 2009 May 19. PMID:19458048<ref>PMID:19458048</ref>
-{{ABSTRACT_PUBMED_19458048}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3fwl" style="background-color:#fffaf0;"></div>
-[[3fwl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FWL OCA].
 ==See Also==
-*[[Penicillin-binding protein|Penicillin-binding protein]]
+*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019458048</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Chou, L Y.]]
+[[Category: Large Structures]]
-[[Category: Huang, C Y.]]
+[[Category: Chou LY]]
-[[Category: Lai, Y T.]]
+[[Category: Huang CY]]
-[[Category: Ma, C.]]
+[[Category: Lai YT]]
-[[Category: Sung, M T.]]
+[[Category: Ma C]]
-[[Category: Wong, C H.]]
+[[Category: Sung MT]]
-[[Category: Alternative initiation]]
+[[Category: Wong CH]]
-[[Category: Antibiotic resistance]]
-[[Category: Antibiotics design]]
-[[Category: Bacterial cell wall synthesis]]
-[[Category: Cell inner membrane]]
-[[Category: Cell membrane]]
-[[Category: Cell shape]]
-[[Category: Cell wall biogenesis/degradation]]
-[[Category: Glycosyltransferase]]
-[[Category: Hydrolase]]
-[[Category: Membrane]]
-[[Category: Multifunctional enzyme]]
-[[Category: Penicillin-binding protein]]
-[[Category: Peptidoglycan synthesis]]
-[[Category: Signal-anchor]]
-[[Category: Transferase]]
-[[Category: Transmembrane]]