3vma: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3vma.jpg|left|200px]]


<!--
==Crystal Structure of the Full-Length Transglycosylase PBP1b from Escherichia coli==
The line below this paragraph, containing "STRUCTURE_3vma", creates the "Structure Box" on the page.
<StructureSection load='3vma' size='340' side='right'caption='[[3vma]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3vma]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fwm 3fwm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VMA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.161&#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></td></tr>
{{STRUCTURE_3vma|  PDB=3vma  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vma OCA], [https://pdbe.org/3vma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vma RCSB], [https://www.ebi.ac.uk/pdbsum/3vma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vma 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).
<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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vma" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19458048}}, adds the Publication Abstract to the page
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19458048 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_19458048}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
[[3vma]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fwm 3fwm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VMA OCA].
[[Category: Large Structures]]
 
[[Category: Cheng WC]]
==Reference==
[[Category: Chou LY]]
<ref group="xtra">PMID:019458048</ref><references group="xtra"/>
[[Category: Huang CY]]
[[Category: Escherichia coli]]
[[Category: Lai YT]]
[[Category: Cheng, W C.]]
[[Category: Ma C]]
[[Category: Chou, L Y.]]
[[Category: Shih HW]]
[[Category: Huang, C Y.]]
[[Category: Sung MT]]
[[Category: Lai, Y T.]]
[[Category: Wong CH]]
[[Category: Ma, C.]]
[[Category: Shih, H W.]]
[[Category: Sung, M T.]]
[[Category: Wong, C H.]]
[[Category: Antibiotics design]]
[[Category: Bacterial cell wall synthesis]]
[[Category: Ftsn]]
[[Category: Hydrolase-antibiotic complex]]
[[Category: Membrane]]
[[Category: Mipa]]
[[Category: Mlta]]
[[Category: Pbp3]]
[[Category: Penicillin-binding protein]]
[[Category: Transferase]]