1xn4: Difference between revisions
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<StructureSection load='1xn4' size='340' side='right'caption='[[1xn4]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='1xn4' size='340' side='right'caption='[[1xn4]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xn4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1xn4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XN4 FirstGlance]. <br> | ||
</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=1xn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xn4 OCA], [https://pdbe.org/1xn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1xn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xn4 ProSAT]</span></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]] 3.8Å</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=1xn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xn4 OCA], [https://pdbe.org/1xn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xn4 RCSB], [https://www.ebi.ac.uk/pdbsum/1xn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xn4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4QGT7_LEIMA Q4QGT7_LEIMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania major]] | ||
[[Category: Caruthers | [[Category: Caruthers J]] | ||
[[Category: Merritt | [[Category: Merritt EA]] | ||
Latest revision as of 09:48, 23 August 2023
PUTATIVE MAR1 RIBONUCLEASE FROM LEISHMANIA MAJORPUTATIVE MAR1 RIBONUCLEASE FROM LEISHMANIA MAJOR
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the crystal structures of three homologous proteins from the pathogenic protozoans Leishmania donovani, Leishmania major, and Trypanosoma cruzi. We propose that these proteins represent a new subfamily within the isochorismatase superfamily (CDD classification cd004310). Their overall fold and key active site residues are structurally homologous both to the biochemically well-characterized N-carbamoylsarcosine-amidohydrolase, a cysteine hydrolase, and to the phenazine biosynthesis protein PHZD (isochorismase), an aspartyl hydrolase. All three proteins are annotated as mitochondrial-associated ribonuclease Mar1, based on a previous characterization of the homologous protein from L. tarentolae. This would constitute a new enzymatic activity for this structural superfamily, but this is not strongly supported by the observed structures. In these protozoan proteins, the extended active site is formed by inter-subunit association within a tetramer, which implies a distinct evolutionary history and substrate specificity from the previously characterized members of the isochorismatase superfamily. The characterization of the active site is supported crystallographically by the presence of an unidentified ligand bound at the active site cysteine of the T. cruzi structure. Crystal structures and proposed structural/functional classification of three protozoan proteins from the isochorismatase superfamily.,Caruthers J, Zucker F, Worthey E, Myler PJ, Buckner F, Van Voorhuis W, Mehlin C, Boni E, Feist T, Luft J, Gulde S, Lauricella A, Kaluzhniy O, Anderson L, Le Trong I, Holmes MA, Earnest T, Soltis M, Hodgson KO, Hol WG, Merritt EA Protein Sci. 2005 Nov;14(11):2887-94. Epub 2005 Sep 30. PMID:16199669[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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