1tdt
From Proteopedia
(New page: 200px<br /><applet load="1tdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tdt, resolution 2.2Å" /> '''THREE-DIMENSIONAL STR...) |
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- | [[Image:1tdt.gif|left|200px]]<br /><applet load="1tdt" size=" | + | [[Image:1tdt.gif|left|200px]]<br /><applet load="1tdt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tdt, resolution 2.2Å" /> | caption="1tdt, resolution 2.2Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINLYTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
- | The conversion of tetrahydrodipicolinate and succinyl-CoA to | + | 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== | ==About this Structure== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Beaman, T | + | [[Category: Beaman, T W.]] |
- | [[Category: Binder, D | + | [[Category: Binder, D W.]] |
- | [[Category: Blanchard, J | + | [[Category: Blanchard, J S.]] |
- | [[Category: Roderick, S | + | [[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]] | ||
- | ''Page seeded by [http:// | + | ''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
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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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