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1nh8

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[[Image:1nh8.gif|left|200px]]<br /><applet load="1nh8" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nh8, resolution 1.80&Aring;" />
 
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'''ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE'''<br />
 
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==Overview==
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==ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE==
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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.
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<StructureSection load='1nh8' size='340' side='right'caption='[[1nh8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NH8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh8 OCA], [https://pdbe.org/1nh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1nh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nh8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIS1_MYCTU HIS1_MYCTU] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nh/1nh8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nh8 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1NH8 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>, <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=HIS:'>HIS</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=1NH8 OCA].
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*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12511575 12511575]
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[[Category: Large Structures]]
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[[Category: ATP phosphoribosyltransferase]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Cho Y]]
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[[Category: Single protein]]
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[[Category: Sacchettini JC]]
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[[Category: Cho, Y.]]
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[[Category: Sharma V]]
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[[Category: Sacchettini, J C.]]
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[[Category: Sharma, V.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: AMP]]
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[[Category: HIS]]
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[[Category: SO4]]
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[[Category: atp]]
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[[Category: de novo his biosynthesis]]
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[[Category: phosphoribosyltransferase]]
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[[Category: protein structure initiative]]
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[[Category: prpp]]
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[[Category: prtase]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:05 2008''
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Current revision

ATP PHOSPHORIBOSYLTRANSFERASE (ATP-PRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AMP AND HISTIDINE

PDB ID 1nh8

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