1x9g

<StructureSection load='1x9g' size='340' side='right' caption='[[1x9g]], [[Resolution|resolution]] 2.41&Aring;' scene=''>

<table><tr><td colspan='2'>[[1x9g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X9G FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x9g OCA], [http://pdbe.org/1x9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x9g RCSB], [http://www.ebi.ac.uk/pdbsum/1x9g PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x9/1x9g_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

We 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<ref>PMID:16199669</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1x9g" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Leido]]

[[Category: Caruthers, J]]

[[Category: Merritt, E A]]

[[Category: Structural genomic]]

[[Category: Unknown function]]