1mp2
From Proteopedia
(New page: 200px<br /><applet load="1mp2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mp2, resolution 2.3Å" /> '''Structure of MT-ADPRa...) |
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| - | [[Image:1mp2.jpg|left|200px]]<br /><applet load="1mp2" size=" | + | [[Image:1mp2.jpg|left|200px]]<br /><applet load="1mp2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mp2, resolution 2.3Å" /> | caption="1mp2, resolution 2.3Å" /> | ||
'''Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis'''<br /> | '''Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nudix hydrolases are a family of proteins that contain the characteristic | + | Nudix hydrolases are a family of proteins that contain the characteristic sequence GX(5)EX(7)REUXEEXG(I/L/V), the Nudix box. They catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives such as ADP-ribose, Ap(n)A (3 </= n </= 6), NADH, and dATP. A number of Nudix hydrolases from several species, ranging from bacteria to humans, have been characterized, including, in some cases, the determination of their three-dimensional structures. The product of the Rv1700 gene of M. tuberculosis is a Nudix hydrolase specific for ADP-ribose (ADPR). We have determined the crystal structures of MT-ADPRase alone, and in complex with substrate, with substrate and the nonactivating metal ion Gd(3+), and in complex with a nonhydrolyzable ADPR analog and the activating metal ion Mn(2+). These structures, refined with data extending to resolutions between 2.0 and 2.3 A, showed that there are sequence differences in binding site residues between MT-ADPRase and a human homolog that may be exploited for antituberculosis drug development. |
==About this Structure== | ==About this Structure== | ||
| - | 1MP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] Full crystallographic information is available from [http:// | + | 1MP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/ADP-ribose_diphosphatase ADP-ribose diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.13 3.6.1.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Bianchet, M | + | [[Category: Bianchet, M A.]] |
| - | [[Category: Cunningham, J | + | [[Category: Cunningham, J E.]] |
| - | [[Category: Gabelli, S | + | [[Category: Gabelli, S B.]] |
| - | [[Category: Handley, S | + | [[Category: Handley, S F.O.]] |
| - | [[Category: Kang, L | + | [[Category: Kang, L W.]] |
[[Category: adpr]] | [[Category: adpr]] | ||
[[Category: adprase]] | [[Category: adprase]] | ||
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[[Category: rv1700]] | [[Category: rv1700]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:33 2008'' |
Revision as of 11:57, 21 February 2008
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Structure of MT-ADPRase (Apoenzyme), a Nudix hydrolase from Mycobacterium tuberculosis
Overview
Nudix hydrolases are a family of proteins that contain the characteristic sequence GX(5)EX(7)REUXEEXG(I/L/V), the Nudix box. They catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives such as ADP-ribose, Ap(n)A (3 </= n </= 6), NADH, and dATP. A number of Nudix hydrolases from several species, ranging from bacteria to humans, have been characterized, including, in some cases, the determination of their three-dimensional structures. The product of the Rv1700 gene of M. tuberculosis is a Nudix hydrolase specific for ADP-ribose (ADPR). We have determined the crystal structures of MT-ADPRase alone, and in complex with substrate, with substrate and the nonactivating metal ion Gd(3+), and in complex with a nonhydrolyzable ADPR analog and the activating metal ion Mn(2+). These structures, refined with data extending to resolutions between 2.0 and 2.3 A, showed that there are sequence differences in binding site residues between MT-ADPRase and a human homolog that may be exploited for antituberculosis drug development.
About this Structure
1MP2 is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as ADP-ribose diphosphatase, with EC number 3.6.1.13 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis., Kang LW, Gabelli SB, Cunningham JE, O'Handley SF, Amzel LM, Structure. 2003 Aug;11(8):1015-23. PMID:12906832
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