6fqb: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6fqb is ~~ON HOLD until Paper~~ Publication

==MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6==

== 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>

== 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.

~~Authors~~:

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>

~~Description~~:

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

[[Category: ~~Unreleased Structures~~]]

</div>

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6fqb is ON HOLD  until Paper Publication
+==MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6==
+<StructureSection load='6fqb' size='340' side='right' caption='[[6fqb]], [[Resolution|resolution]] 3.00&Aring;' 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]