6fqb: Difference between revisions
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==MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6== | |||
<StructureSection load='6fqb' size='340' side='right' caption='[[6fqb]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fqb]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FQB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylcobyric_acid_synthase_(glutamine-hydrolyzing) Adenosylcobyric acid synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.10 6.3.5.10] </span></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=6fqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fqb OCA], [http://pdbe.org/6fqb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fqb RCSB], [http://www.ebi.ac.uk/pdbsum/6fqb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fqb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 A resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies. | |||
Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.,Morlot C, Straume D, Peters K, Hegnar OA, Simon N, Villard AM, Contreras-Martel C, Leisico F, Breukink E, Gravier-Pelletier C, Le Corre L, Vollmer W, Pietrancosta N, Havarstein LS, Zapun A Nat Commun. 2018 Aug 9;9(1):3180. doi: 10.1038/s41467-018-05602-w. PMID:30093673<ref>PMID:30093673</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fqb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Breukink, E]] | |||
[[Category: Contreras-Martel, C]] | |||
[[Category: Corre, L Le]] | |||
[[Category: Gravier-Pelletier, C]] | |||
[[Category: Havarstein, L S]] | |||
[[Category: Hegnar, O A]] | |||
[[Category: Leisico, F]] | |||
[[Category: Morlot, C]] | |||
[[Category: Peters, K]] | |||
[[Category: Pietrancosta, N]] | |||
[[Category: Simon, N]] | |||
[[Category: Straume, D]] | |||
[[Category: Villard, A M]] | |||
[[Category: Vollmer, W]] | |||
[[Category: Zapun, A]] | |||
[[Category: Amidotransferase]] | |||
[[Category: Cytosolic]] | |||
[[Category: Ligase]] | |||
[[Category: Mur family]] | |||
Revision as of 09:11, 22 August 2018
MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6
Structural highlights
Publication Abstract from PubMedThe universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 A resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.,Morlot C, Straume D, Peters K, Hegnar OA, Simon N, Villard AM, Contreras-Martel C, Leisico F, Breukink E, Gravier-Pelletier C, Le Corre L, Vollmer W, Pietrancosta N, Havarstein LS, Zapun A Nat Commun. 2018 Aug 9;9(1):3180. doi: 10.1038/s41467-018-05602-w. PMID:30093673[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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