4o96
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4o96]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._Sakai Escherichia coli O157:H7 str. Sakai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O96 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4o96]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._Sakai Escherichia coli O157:H7 str. Sakai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O96 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.6Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4o96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o96 OCA], [https://pdbe.org/4o96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o96 RCSB], [https://www.ebi.ac.uk/pdbsum/4o96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o96 ProSAT]</span></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=4o96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o96 OCA], [https://pdbe.org/4o96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o96 RCSB], [https://www.ebi.ac.uk/pdbsum/4o96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o96 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8XAL6_ECO57 Q8XAL6_ECO57] | [https://www.uniprot.org/uniprot/Q8XAL6_ECO57 Q8XAL6_ECO57] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of a C-terminal domain of enterohemorrhagic Escherichia coli type III effector NleH2 has been determined to 2.6 A resolution. The structure resembles those of protein kinases featuring the catalytic, activation, and glycine-rich loop motifs and ATP-binding site. The position of helix alphaC and the lack of a conserved arginine within an equivalent HRD motif suggested that the NleH2 kinase domain's active conformation might not require phosphorylation. The activation segment markedly contributed to the dimerization interface of NleH2, which can also accommodate the NleH1-NleH2 heterodimer. The C-terminal PDZ-binding motif of NleH2 provided bases for interaction with host proteins. | ||
| - | |||
| - | Type III Effector NleH2 from Escherichia coli O157:H7 str. Sakai Features an Atypical Protein Kinase Domain.,Halavaty AS, Anderson SM, Wawrzak Z, Kudritska M, Skarina T, Anderson WF, Savchenko A Biochemistry. 2014 Apr 10. PMID:24712300<ref>PMID:24712300</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4o96" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
2.60 Angstrom resolution crystal structure of a protein kinase domain of type III effector NleH2 (ECs1814) from Escherichia coli O157:H7 str. Sakai
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