1nh7
From Proteopedia
(New page: 200px<br /><applet load="1nh7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nh7, resolution 2.70Å" /> '''ATP PHOSPHORIBOSYLTR...) |
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| - | [[Image:1nh7.gif|left|200px]]<br /><applet load="1nh7" size=" | + | [[Image:1nh7.gif|left|200px]]<br /><applet load="1nh7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nh7, resolution 2.70Å" /> | caption="1nh7, resolution 2.70Å" /> | ||
'''ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | '''ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of | + | The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 A resolution and without ligands to 2.7 A resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures. |
==About this Structure== | ==About this Structure== | ||
| - | 1NH7 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 SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] Full crystallographic information is available from [http:// | + | 1NH7 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=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NH7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cho, Y.]] | [[Category: Cho, Y.]] | ||
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
[[Category: Sharma, V.]] | [[Category: Sharma, V.]] | ||
| - | [[Category: TBSGC, TB | + | [[Category: TBSGC, TB Structural Genomics Consortium.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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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 14:06:02 2008'' |
Revision as of 12:06, 21 February 2008
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ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS
Overview
The N-1-(5'-phosphoribosyl)-ATP transferase catalyzes the first step of the histidine biosynthetic pathway and is regulated by a feedback mechanism by the product histidine. The crystal structures of the N-1-(5'-phosphoribosyl)-ATP transferase from Mycobacterium tuberculosis in complex with inhibitor histidine and AMP has been determined to 1.8 A resolution and without ligands to 2.7 A resolution. The active enzyme exists primarily as a dimer, and the histidine-inhibited form is a hexamer. The structure represents a new fold for a phosphoribosyltransferase, consisting of three continuous domains. The inhibitor AMP binds in the active site cavity formed between the two catalytic domains. A model for the mechanism of allosteric inhibition has been derived from conformational differences between the AMP:His-bound and apo structures.
About this Structure
1NH7 is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Active as ATP phosphoribosyltransferase, with EC number 2.4.2.17 Full crystallographic information is available from OCA.
Reference
Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis., Cho Y, Sharma V, Sacchettini JC, J Biol Chem. 2003 Mar 7;278(10):8333-9. Epub 2003 Jan 2. PMID:12511575
Page seeded by OCA on Thu Feb 21 14:06:02 2008
Categories: ATP phosphoribosyltransferase | Mycobacterium tuberculosis | Single protein | Cho, Y. | Sacchettini, J C. | Sharma, V. | TBSGC, TB Structural Genomics Consortium. | MG | SO4 | Atp | De novo his biosynthesis | Phosphoribosyltransferase | Protein structure initiative | Prpp | Prtase | Psi | Structural genomics | Tb structural genomics consortium | Tbsgc | Transferase
