This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1mk1
From Proteopedia
(New page: 200px<br /><applet load="1mk1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mk1, resolution 2.0Å" /> '''Structure of the MT-A...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mk1.jpg|left|200px]]<br /><applet load="1mk1" size=" | + | [[Image:1mk1.jpg|left|200px]]<br /><applet load="1mk1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mk1, resolution 2.0Å" /> | caption="1mk1, resolution 2.0Å" /> | ||
'''Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme'''<br /> | '''Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme'''<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== | ||
| - | 1MK1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with APR as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1MK1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=APR:'>APR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1MK1 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[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: APR]] | [[Category: APR]] | ||
[[Category: adenosine diphospho-ribose]] | [[Category: adenosine diphospho-ribose]] | ||
| Line 28: | Line 28: | ||
[[Category: rv1700]] | [[Category: rv1700]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:01 2008'' |
Revision as of 11:56, 21 February 2008
|
Structure of the MT-ADPRase in complex with ADPR, a Nudix enzyme
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
1MK1 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. 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
Page seeded by OCA on Thu Feb 21 13:56:01 2008
