2rjs: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 15: Line 15:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjs_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjs_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>

Latest revision as of 11:39, 30 October 2024

SgTAM bound to substrate mimicSgTAM bound to substrate mimic

Structural highlights

2rjs is a 2 chain structure with sequence from Streptomyces globisporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TAM_STRGL Involved in the biosynthesis of the enediyne antitumor antibiotic C-1027. Catalyzes the MIO-dependent deamination of L-tyrosine generating the corresponding alpha,beta-unsaturated acid, (S)-beta-tyrosine.[1] [2] [3]

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 PubMed

The synthesis and evaluation of two classes of inhibitors for SgTAM, a 4-methylideneimidazole-5-one (MIO) containing tyrosine aminomutase, are described. A mechanism-based strategy was used to design analogs that mimic the substrate or product of the reaction and form covalent interactions with the enzyme through the MIO prosthetic group. The analogs were characterized by measuring inhibition constants and X-ray crystallographic structural analysis of the co-complexes bound to the aminomutase, SgTAM.

Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM.,Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Liu W, Christenson SD, Standage S, Shen B. Biosynthesis of the enediyne antitumor antibiotic C-1027. Science. 2002 Aug 16;297(5584):1170-3. PMID:12183628 doi:10.1126/science.1072110
  2. Christianson CV, Montavon TJ, Van Lanen SG, Shen B, Bruner SD. The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway. Biochemistry. 2007 Jun 19;46(24):7205-14. Epub 2007 May 22. PMID:17516659 doi:10.1021/bi7003685
  3. Cooke HA, Bruner SD. Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites. Biopolymers. 2010 Sep;93(9):802-10. PMID:20577998 doi:10.1002/bip.21500
  4. Montavon TJ, Christianson CV, Festin GM, Shen B, Bruner SD. Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM. Bioorg Med Chem Lett. 2008 May 15;18(10):3099-102. Epub 2007 Nov 19. PMID:18078753 doi:10.1016/j.bmcl.2007.11.046

2rjs, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA