1tdt: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tdt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium 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 [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 [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TDT FirstGlance]. <br> | ||
</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=1tdt RCSB], [http://www.ebi.ac.uk/pdbsum/1tdt PDBsum]</span></td></tr> | </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://www.rcsb.org/pdb/explore.do?structureId=1tdt RCSB], [http://www.ebi.ac.uk/pdbsum/1tdt PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== 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). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mycobacterium bovis]] | [[Category: Mycobacterium bovis]] | ||
[[Category: Beaman, T W | [[Category: Beaman, T W]] | ||
[[Category: Binder, D W | [[Category: Binder, D W]] | ||
[[Category: Blanchard, J S | [[Category: Blanchard, J S]] | ||
[[Category: Roderick, S L | [[Category: Roderick, S L]] | ||
[[Category: Cell wall biosynthesis]] | [[Category: Cell wall biosynthesis]] | ||
[[Category: Hexapeptide transferase]] | [[Category: Hexapeptide transferase]] | ||
Revision as of 03:01, 25 December 2014
THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASETHREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE
Structural highlights
Function[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). 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 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., & 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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