1tdt: Difference between revisions

Revision as of 03:58, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tdt.png

Template:STRUCTURE 1tdt

THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASETHREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE

Template:ABSTRACT PUBMED 9012664

About this StructureAbout this Structure

1TDT is a Single protein structure of sequence from Mycobacterium bovis. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 03:58:32 2008

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

OCA

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-[[Image:1tdt.gif|left|200px]]
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 {{STRUCTURE_1tdt|  PDB=1tdt  |  SCENE=  }}
-'''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE'''
+===THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9012664}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9012664 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9012664}}
 ==About this Structure==
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 [[Category: Succinyltransferase]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:49:57 2008''
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