2olv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:20, 28 December 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2olv.jpg|left|200px]]
 
-
{{Structure
+
==Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex==
-
|PDB= 2olv |SIZE=350|CAPTION= <scene name='initialview01'>2olv</scene>, resolution 2.800&Aring;
+
<StructureSection load='2olv' size='340' side='right'caption='[[2olv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
+
<table><tr><td colspan='2'>[[2olv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OLV FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-
|GENE= pbp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0E:MOENOMYCIN'>M0E</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2olv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olv OCA], [https://pdbe.org/2olv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2olv RCSB], [https://www.ebi.ac.uk/pdbsum/2olv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2olv ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[2olu|2OLU]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2olv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olv OCA], [http://www.ebi.ac.uk/pdbsum/2olv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2olv RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/Q9R744_STAAU Q9R744_STAAU]
 +
== 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/ol/2olv_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/main_output.php?pdb_ID=2olv ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.
-
'''Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex'''
+
Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis.,Lovering AL, de Castro LH, Lim D, Strynadka NC Science. 2007 Mar 9;315(5817):1402-5. PMID:17347437<ref>PMID:17347437</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2olv" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all bacteria. Long considered the "holy grail" of antibiotic research, they represent an essential and easily accessible drug target for antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus. We have determined the 2.8 angstrom structure of a bifunctional cell-wall cross-linking enzyme, including its transpeptidase and GT domains, both unliganded and complexed with the substrate analog moenomycin. The peptidoglycan GTs adopt a fold distinct from those of other GT classes. The structures give insight into critical features of the catalytic mechanism and key interactions required for enzyme inhibition.
+
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2OLV is a [[Single protein]] structure of 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=2OLV OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis., Lovering AL, de Castro LH, Lim D, Strynadka NC, Science. 2007 Mar 9;315(5817):1402-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17347437 17347437]
+
-
[[Category: Single protein]]
+
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
-
[[Category: Castro, L De.]]
+
[[Category: De Castro L]]
-
[[Category: Lim, D.]]
+
[[Category: Lim D]]
-
[[Category: Lovering, A L.]]
+
[[Category: Lovering AL]]
-
[[Category: Strynadka, N C.J.]]
+
[[Category: Strynadka NCJ]]
-
[[Category: glycosyltransferase family 51]]
+
-
[[Category: lysozyme fold]]
+
-
[[Category: transpeptidase fold]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:19:44 2008''
+

Current revision

Structural Insight Into the Transglycosylation Step Of Bacterial Cell Wall Biosynthesis : Donor Ligand Complex

PDB ID 2olv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2olv"
Personal tools