7omj: Difference between revisions

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 <StructureSection load='7omj' size='340' side='right'caption='[[7omj]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7omj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OMJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7omj]] is a 1 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=7OMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OMJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=7omj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7omj OCA], [https://pdbe.org/7omj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7omj RCSB], [https://www.ebi.ac.uk/pdbsum/7omj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7omj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FTSZ_STAAU FTSZ_STAAU]] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]
+[https://www.uniprot.org/uniprot/FTSZ_STAA8 FTSZ_STAA8] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]<ref>PMID:14617148</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Treadmilling protein filaments perform essential cellular functions by growing from one end while shrinking from the other, driven by nucleotide hydrolysis. Bacterial cell division relies on the primitive tubulin homolog FtsZ, a target for antibiotic discovery that assembles into single treadmilling filaments that hydrolyse GTP at an active site formed upon subunit association. We determined high-resolution filament structures of FtsZ from the pathogen Staphylococcus aureus in complex with different nucleotide analogs and cations, including mimetics of the ground and transition states of catalysis. Together with mutational and biochemical analyses, our structures reveal interactions made by the GTP gamma-phosphate and Mg2+ at the subunit interface, a K+ ion stabilizing loop T7 for co-catalysis, new roles of key residues at the active site and a nearby crosstalk area, and rearrangements of a dynamic water shell bridging adjacent subunits upon GTP hydrolysis. We propose a mechanistic model that integrates nucleotide hydrolysis signaling with assembly-associated conformational changes and filament treadmilling. Equivalent assembly mechanisms may apply to more complex tubulin and actin cytomotive filaments that share analogous features with FtsZ.
-FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics.,Ruiz FM, Huecas S, Santos-Aledo A, Prim EA, Andreu JM, Fernandez-Tornero C PLoS Biol. 2022 Mar 21;20(3):e3001497. doi: 10.1371/journal.pbio.3001497., eCollection 2022 Mar. PMID:35312677<ref>PMID:35312677</ref>
+==See Also==
+*[[Cell division protein 3D structures|Cell division protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7omj" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 23: / Line 18: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Andreu, J M]]
+[[Category: Staphylococcus aureus]]
-[[Category: Fernandez-Tornero, C]]
+[[Category: Andreu JM]]
-[[Category: Ruiz, F M]]
+[[Category: Fernandez-Tornero C]]
-[[Category: Cell cycle]]
+[[Category: Ruiz FM]]
-[[Category: Cell division protein]]