2lf3

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[[2lf3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._maculicola Pseudomonas syringae pv. maculicola]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LF3 OCA]. <br>
[[2lf3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._maculicola Pseudomonas syringae pv. maculicola]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LF3 OCA]. <br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lf3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lf3 RCSB], [http://www.ebi.ac.uk/pdbsum/2lf3 PDBsum]</span><br>
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
HopPmaL is a member of the HopAB family of type III effectors present in the phytopathogen Pseudomonas syringae. Using both X-ray crystallography and solution nuclear magnetic resonance, we demonstrate that HopPmaL contains two structurally homologous yet functionally distinct domains. The N-terminal domain corresponds to the previously described Pto-binding domain, while the previously uncharacterised C-terminal domain spans residues 308-385. While structurally similar, these domains do not share significant sequence similarity and most importantly demonstrate significant differences in key residues involved in host protein recognition, suggesting that each of them targets a different host protein.
HopPmaL is a member of the HopAB family of type III effectors present in the phytopathogen Pseudomonas syringae. Using both X-ray crystallography and solution nuclear magnetic resonance, we demonstrate that HopPmaL contains two structurally homologous yet functionally distinct domains. The N-terminal domain corresponds to the previously described Pto-binding domain, while the previously uncharacterised C-terminal domain spans residues 308-385. While structurally similar, these domains do not share significant sequence similarity and most importantly demonstrate significant differences in key residues involved in host protein recognition, suggesting that each of them targets a different host protein.

Revision as of 10:27, 30 April 2014

Solution NMR structure of HopPmaL_281_385 from Pseudomonas syringae pv. maculicola str. ES4326, Midwest Center for Structural Genomics target APC40104.5 and Northeast Structural Genomics Consortium target PsT2A

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