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==Identification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer==
==Identification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer==
<StructureSection load='3dwk' size='340' side='right' caption='[[3dwk]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='3dwk' size='340' side='right'caption='[[3dwk]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dwk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DWK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dwk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DWK FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 3.1&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2olu|2olu]], [[2olv|2olv]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pbp2, SACOL1490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])</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=3dwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dwk OCA], [https://pdbe.org/3dwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dwk RCSB], [https://www.ebi.ac.uk/pdbsum/3dwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dwk ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dwk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dwk RCSB], [http://www.ebi.ac.uk/pdbsum/3dwk PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/Q8KHY3_STAAU Q8KHY3_STAAU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/3dwk_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dw/3dwk_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3dwk ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3dwk" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Penicillin-binding protein|Penicillin-binding protein]]
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Staphylococcus aureus]]
[[Category: Large Structures]]
[[Category: Castro, L De.]]
[[Category: Staphylococcus aureus subsp. aureus COL]]
[[Category: Lovering, A L.]]
[[Category: De Castro L]]
[[Category: Strynadka, N C.J.]]
[[Category: Lovering AL]]
[[Category: Cell shape]]
[[Category: Strynadka NCJ]]
[[Category: Cell wall biogenesis/degradation]]
[[Category: Lysozyme-fold transpeptidase fold pi-helix]]
[[Category: Membrane]]
[[Category: Peptidoglycan synthesis]]
[[Category: Transferase]]

Latest revision as of 15:53, 30 August 2023

Identification of Dynamic Structural Motifs Involved in Peptidoglycan GlycosyltransferIdentification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer

Structural highlights

3dwk is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus COL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8KHY3_STAAU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have determined the structure of a new form of the bifunctional peptidoglycan glycosyltransferase (GT)/transpeptidase penicillin-binding protein 2 from the pathogen Staphylococcus aureus. We observe several previously unstructured regions of the GT substrate-binding pockets, including a pi-bulge in the outer helix that may be responsible for the conformational flexibility of active-site motifs required for transfer of product to the donor binding site during processive rounds of peptidoglycan polymerization. The identification of a beta-hairpin in the usually unstructured region of the fold shares local structural homology to that of an exomuramidase, heightening comparisons between this biosynthetic enzyme and lytic peptidoglycan transglycosylases. This new form also shows remarkable interdomain flexibility, causing the linker region of the fold to project into the GT active site. This self-interaction may have significant consequences for the regulation of polymerization activity. The derived information is used to build a catalytic model of both donor and acceptor glycolipid substrates.

Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer.,Lovering AL, De Castro L, Strynadka NC J Mol Biol. 2008 Oct 31;383(1):167-77. Epub 2008 Aug 19. PMID:18760285[1]

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

See Also

References

  1. Lovering AL, De Castro L, Strynadka NC. Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer. J Mol Biol. 2008 Oct 31;383(1):167-77. Epub 2008 Aug 19. PMID:18760285 doi:10.1016/j.jmb.2008.08.020

3dwk, resolution 3.10Å

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OCA