2rjs: Difference between revisions

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{{Seed}}
[[Image:2rjs.png|left|200px]]


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==SgTAM bound to substrate mimic==
The line below this paragraph, containing "STRUCTURE_2rjs", creates the "Structure Box" on the page.
<StructureSection load='2rjs' size='340' side='right'caption='[[2rjs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2rjs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_globisporus Streptomyces globisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJS FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=296:(3R)-3-AMINO-2,2-DIFLUORO-3-(4-METHOXYPHENYL)PROPANOIC+ACID'>296</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></td></tr>
{{STRUCTURE_2rjs|  PDB=2rjs  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjs OCA], [https://pdbe.org/2rjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rjs RCSB], [https://www.ebi.ac.uk/pdbsum/2rjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TAM_STRGL 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.<ref>PMID:12183628</ref> <ref>PMID:17516659</ref> <ref>PMID:20577998</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2rjs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===SgTAM bound to substrate mimic===
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<ref>PMID:18078753</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rjs" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18078753}}, adds the Publication Abstract to the page
*[[Aminomutase 3D structures|Aminomutase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18078753 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_18078753}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2RJS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_globisporus Streptomyces globisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJS OCA].
 
==Reference==
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. 2007 Nov 19;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18078753 18078753]
[[Category: Single protein]]
[[Category: Streptomyces globisporus]]
[[Category: Streptomyces globisporus]]
[[Category: Tyrosine 2,3-aminomutase]]
[[Category: Bruner SD]]
[[Category: Bruner, S D.]]
[[Category: Christianson CV]]
[[Category: Christianson, C V.]]
[[Category: Montavon TJ]]
[[Category: Montavon, T J.]]
[[Category: 4-methylidene imidazole]]
[[Category: Aminomutase]]
[[Category: C-1027]]
[[Category: Isomerase]]
[[Category: Mio]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 10:05:30 2008''

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

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