3l7m: Difference between revisions
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==Structure of the Wall Teichoic Acid Polymerase TagF, H548A== | |||
<StructureSection load='3l7m' size='340' side='right' caption='[[3l7m]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
{ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3l7m]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_epidermidis Staphylococcus epidermidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L7M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L7M FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDT:{[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC+ACID'>EDT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l7i|3l7i]], [[3l7j|3l7j]], [[3l7k|3l7k]], [[3l7l|3l7l]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SERP1960, tagF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1282 Staphylococcus epidermidis])</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=3l7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l7m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l7m RCSB], [http://www.ebi.ac.uk/pdbsum/3l7m PDBsum]</span></td></tr> | |||
</table> | |||
== 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/l7/3l7m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Teichoic acid polymers are composed of polyol-phosphate units and form a major component of Gram-positive bacterial cell walls. These anionic compounds perform a multitude of important roles in bacteria and are synthesized by monotopic membrane proteins of the TagF polymerase family. We have determined the structure of Staphylococcus epidermidis TagF to 2.7-A resolution from a construct that includes both the membrane-targeting region and the glycerol-phosphate polymerase domains. TagF possesses a helical region for interaction with the lipid bilayer, placing the active site at a suitable distance for access to the membrane-bound substrate. Characterization of active-site residue variants and analysis of a CDP-glycerol substrate complex suggest a mechanism for polymer synthesis. With the importance of teichoic acid in Gram-positive physiology, this elucidation of the molecular details of TagF function provides a critical new target in the development of novel anti-infectives. | |||
Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis.,Lovering AL, Lin LY, Sewell EW, Spreter T, Brown ED, Strynadka NC Nat Struct Mol Biol. 2010 May;17(5):582-9. Epub 2010 Apr 18. PMID:20400947<ref>PMID:20400947</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Staphylococcus epidermidis]] | [[Category: Staphylococcus epidermidis]] | ||
[[Category: Lovering, A L | [[Category: Lovering, A L]] | ||
[[Category: Strynadka, N C.J | [[Category: Strynadka, N C.J]] | ||
[[Category: Gt-b fold]] | [[Category: Gt-b fold]] | ||
[[Category: Monotopic membrane protein]] | [[Category: Monotopic membrane protein]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] |
Revision as of 19:37, 18 December 2014
Structure of the Wall Teichoic Acid Polymerase TagF, H548AStructure of the Wall Teichoic Acid Polymerase TagF, H548A
Structural highlights
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 PubMedTeichoic acid polymers are composed of polyol-phosphate units and form a major component of Gram-positive bacterial cell walls. These anionic compounds perform a multitude of important roles in bacteria and are synthesized by monotopic membrane proteins of the TagF polymerase family. We have determined the structure of Staphylococcus epidermidis TagF to 2.7-A resolution from a construct that includes both the membrane-targeting region and the glycerol-phosphate polymerase domains. TagF possesses a helical region for interaction with the lipid bilayer, placing the active site at a suitable distance for access to the membrane-bound substrate. Characterization of active-site residue variants and analysis of a CDP-glycerol substrate complex suggest a mechanism for polymer synthesis. With the importance of teichoic acid in Gram-positive physiology, this elucidation of the molecular details of TagF function provides a critical new target in the development of novel anti-infectives. Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis.,Lovering AL, Lin LY, Sewell EW, Spreter T, Brown ED, Strynadka NC Nat Struct Mol Biol. 2010 May;17(5):582-9. Epub 2010 Apr 18. PMID:20400947[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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