3h5e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==LeuD_1-156 small subunit of isopropylmalate isomerase (Rv2987c) from mycobacterium tuberculosis== | ==LeuD_1-156 small subunit of isopropylmalate isomerase (Rv2987c) from mycobacterium tuberculosis== | ||
<StructureSection load='3h5e' size='340' side='right' caption='[[3h5e]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3h5e' size='340' side='right' caption='[[3h5e]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3h5e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3h5e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H5E FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h5h|3h5h]], [[3h5j|3h5j]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h5h|3h5h]], [[3h5j|3h5j]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2987c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2987c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydratase 3-isopropylmalate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.33 4.2.1.33] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydratase 3-isopropylmalate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.33 4.2.1.33] </span></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=3h5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h5e RCSB], [http://www.ebi.ac.uk/pdbsum/3h5e PDBsum]</span></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=3h5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h5e OCA], [http://pdbe.org/3h5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h5e RCSB], [http://www.ebi.ac.uk/pdbsum/3h5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h5e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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/main_output.php?pdb_ID=3h5e ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 28: | Line 29: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3h5e" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]] | *[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]] | ||
*[[Isopropylmalate isomerase|Isopropylmalate isomerase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: 3-isopropylmalate dehydratase]] | [[Category: 3-isopropylmalate dehydratase]] | ||
[[Category: Geerlof, A]] | [[Category: Geerlof, A]] | ||
[[Category: Manikandan, K]] | [[Category: Manikandan, K]] | ||
Revision as of 23:35, 5 August 2016
LeuD_1-156 small subunit of isopropylmalate isomerase (Rv2987c) from mycobacterium tuberculosisLeuD_1-156 small subunit of isopropylmalate isomerase (Rv2987c) from mycobacterium tuberculosis
Structural highlights
Function[LEUD_MYCTU] Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe absence of the leucine biosynthesis pathway in humans makes the enzymes of this pathway in pathogenic bacteria such as Mycobacterium tuberculosis potential candidates for developing novel antibacterial drugs. One of these enzymes is isopropylmalate isomerase (IPMI). IPMI exists as a complex of two subunits: the large (LeuC) and the small (LeuD) subunit. The functional LeuCD complex catalyzes the stereospecific conversion reaction of alpha-isopropylmalate to beta-isopropylmalate. Three C-terminally truncated variants of LeuD have been analyzed by X-ray crystallography to resolutions of 2.0 A (LeuD_1-156), 1.2 A (LeuD_1-168), and 2.5 A (LeuD_1-186), respectively. The two most flexible parts of the structure are the regions of residues 30-37, the substrate discriminating loop, and of residues 70-74, the substrate binding loop. The three determined structures were also compared with the structures of other bacterial LeuDs. This comparison suggests the presence of two LeuD subfamilies. A model for the structure of the inactive enzyme complex has been obtained from solution X-ray scattering experiments. The crystal structure of LeuD was shown to be compatible with the solution X-ray scattering data from the small subunit. In contrast, the solution scattering results suggest that the large subunit LeuC and the LeuCD complex have overall shapes, which are radically different from the ones observed in the crystals of the functional homolog mitochondrial aconitase. Proteins 2010. (c) 2010 Wiley-Liss, Inc. Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis.,Manikandan K, Geerlof A, Zozulya AV, Svergun DI, Weiss MS Proteins. 2010 Aug 19. PMID:20938981[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||