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1htq

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==Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis==
==Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis==
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<StructureSection load='1htq' size='340' side='right' caption='[[1htq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='1htq' size='340' side='right'caption='[[1htq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1htq]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1htq]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hto|1hto]]</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </span></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=1htq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htq OCA], [https://pdbe.org/1htq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htq RCSB], [https://www.ebi.ac.uk/pdbsum/1htq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htq ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htq OCA], [http://pdbe.org/1htq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1htq RCSB], [http://www.ebi.ac.uk/pdbsum/1htq PDBsum]</span></td></tr>
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</table>
</table>
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{{Large structure}}
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== Function ==
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[https://www.uniprot.org/uniprot/GLN1B_MYCTU GLN1B_MYCTU] Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:7937767, PubMed:12819079). Also able to use GTP (PubMed:7937767). D-glutamate is a poor substrate, and DL-glutamate shows about 50% of the standard specific activity (PubMed:7937767). Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion (PubMed:7937767, PubMed:12819079). Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG) (PubMed:7937767, PubMed:10618433). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (Probable).<ref>PMID:10618433</ref> <ref>PMID:12819079</ref> <ref>PMID:7937767</ref> <ref>PMID:9278431</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1htq_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1htq_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
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*[[Glutamine Synthase|Glutamine Synthase]]
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*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate--ammonia ligase]]
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[[Category: Large Structures]]
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[[Category: Eisenberg, D]]
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[[Category: Gill, H S]]
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[[Category: Pfluegl, G M]]
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[[Category: Structural genomic]]
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[[Category: Glutamine synthetase]]
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[[Category: Ligase]]
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[[Category: Multicopy refinement]]
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Eisenberg D]]
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[[Category: Tbsgc]]
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[[Category: Gill HS]]
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[[Category: Pfluegl GM]]

Current revision

Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis

PDB ID 1htq

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