1f8i: Difference between revisions

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[[Image:1f8i.~~gif~~|left|200px]]

[[Image:1f8i.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS~~'''~~

===CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS===

~~==Overview==~~

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~~Isocitrate lyase (ICL) plays a pivotal role in~~ the persistence of Mycobacterium tuberculosis in mice by sustaining intracellular infection in inflammatory macrophages. The enzyme allows net carbon gain by diverting acetyl-CoA from beta-oxidation of fatty acids into the ~~glyoxylate shunt pathway~~. ~~Given its potential as a drug target against persistent infections, we solved its structure without ligand and in complex with two inhibitors~~. ~~Covalent modification of an active site residue, Cys 191~~, by the ~~inhibitor 3~~-~~bromopyruvate traps the enzyme in a catalytic conformation with the active site completely inaccessible to solvent. The structure of a C191S mutant of the enzyme with the inhibitor 3~~-~~nitropropionate provides further insight into the reaction mechanism.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10932251}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10932251 is the PubMed ID number.

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==About this Structure==

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[[Category: Tb structural genomics consortium]]

[[Category: Tbsgc]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 16~~:01:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:52:05 2008''

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-[[Image:1f8i.gif|left|200px]]
+{{Seed}}
+[[Image:1f8i.png|left|200px]]
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 {{STRUCTURE_1f8i|  PDB=1f8i  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS'''
+===CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS===
-==Overview==
+<!--
-Isocitrate lyase (ICL) plays a pivotal role in the persistence of Mycobacterium tuberculosis in mice by sustaining intracellular infection in inflammatory macrophages. The enzyme allows net carbon gain by diverting acetyl-CoA from beta-oxidation of fatty acids into the glyoxylate shunt pathway. Given its potential as a drug target against persistent infections, we solved its structure without ligand and in complex with two inhibitors. Covalent modification of an active site residue, Cys 191, by the inhibitor 3-bromopyruvate traps the enzyme in a catalytic conformation with the active site completely inaccessible to solvent. The structure of a C191S mutant of the enzyme with the inhibitor 3-nitropropionate provides further insight into the reaction mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_10932251}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10932251 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10932251}}
 ==About this Structure==
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 [[Category: Tb structural genomics consortium]]
 [[Category: Tbsgc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:01:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:52:05 2008''