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<StructureSection load='1tdt' size='340' side='right'caption='[[1tdt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1tdt' size='340' side='right'caption='[[1tdt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tdt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_tuberculosis_typus_bovinus"_lehmann_and_neumann_1907 "mycobacterium tuberculosis typus bovinus" lehmann and neumann 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TDT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1tdt]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_variant_bovis Mycobacterium tuberculosis variant bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TDT 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=1tdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdt OCA], [http://pdbe.org/1tdt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tdt RCSB], [http://www.ebi.ac.uk/pdbsum/1tdt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tdt ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdt OCA], [https://pdbe.org/1tdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tdt RCSB], [https://www.ebi.ac.uk/pdbsum/1tdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tdt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DAPD_MYCBO DAPD_MYCBO]] Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA (By similarity).
[https://www.uniprot.org/uniprot/DAPD_UNKP DAPD_UNKP]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1tdt ConSurf].
</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=1tdt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA is catalyzed by tetrahydrodipicolinate N-succinyltransferase and is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The X-ray crystal structure of THDP succinyltransferase has been determined to 2.2 A resolution and has been refined to a crystallographic R-factor of 17.0%. The enzyme is trimeric and displays the left-handed parallel beta-helix (L beta H) structural motif encoded by the "hexapeptide repeat" amino acid sequence motif [Raetz, C.R.H., &amp; Roderick, S.L. (1995) Science 270, 997-1000]. The approximate location of the active site of THDP succinyltransferase is suggested by the proximity of binding sites for two inhibitors: p-(chloromercuri)benzenesulfonic acid and cobalt ion, both of which bind to the L beta H domain.
Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.,Beaman TW, Binder DA, Blanchard JS, Roderick SL Biochemistry. 1997 Jan 21;36(3):489-94. PMID:9012664<ref>PMID:9012664</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tdt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium tuberculosis typus bovinus lehmann and neumann 1907]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Beaman, T W]]
[[Category: Mycobacterium tuberculosis variant bovis]]
[[Category: Binder, D W]]
[[Category: Beaman TW]]
[[Category: Blanchard, J S]]
[[Category: Binder DW]]
[[Category: Roderick, S L]]
[[Category: Blanchard JS]]
[[Category: Cell wall biosynthesis]]
[[Category: Roderick SL]]
[[Category: Hexapeptide transferase]]
[[Category: Lysine metabolism]]
[[Category: Succinyltransferase]]
[[Category: Transferase]]

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