1tdt

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(New page: 200px<br /><applet load="1tdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tdt, resolution 2.2&Aring;" /> '''THREE-DIMENSIONAL STR...)
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'''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1TDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_bovis Mycobacterium bovis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TDT OCA].
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1TDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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].
==Reference==
==Reference==
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[[Category: Mycobacterium bovis]]
[[Category: Mycobacterium bovis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beaman, T.W.]]
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[[Category: Beaman, T W.]]
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[[Category: Binder, D.W.]]
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[[Category: Binder, D W.]]
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[[Category: Blanchard, J.S.]]
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[[Category: Blanchard, J S.]]
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[[Category: Roderick, S.L.]]
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[[Category: Roderick, S L.]]
[[Category: cell wall biosynthesis]]
[[Category: cell wall biosynthesis]]
[[Category: hexapeptide transferase]]
[[Category: hexapeptide transferase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:33 2008''

Revision as of 13:12, 21 February 2008


1tdt, resolution 2.2Å

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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., & 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.

About this Structure

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

Reference

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

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