3zxr

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Current revision (11:15, 20 December 2023) (edit) (undo)
 
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<StructureSection load='3zxr' size='340' side='right'caption='[[3zxr]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3zxr' size='340' side='right'caption='[[3zxr]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3zxr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZXR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3zxr]] is a 6 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=3ZXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZXR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IQ1:3-(2-TERT-BUTYL-5-(PYRIDIN-4-YL)-1H-IMIDAZOL-4-YL)QUINOLINE'>IQ1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hto|1hto]], [[1htq|1htq]], [[2whi|2whi]], [[2bvc|2bvc]], [[2wgs|2wgs]], [[3zxv|3zxv]]</div></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IQ1:3-(2-TERT-BUTYL-5-(PYRIDIN-4-YL)-1H-IMIDAZOL-4-YL)QUINOLINE'>IQ1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [https://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=3zxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zxr OCA], [https://pdbe.org/3zxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zxr RCSB], [https://www.ebi.ac.uk/pdbsum/3zxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zxr ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zxr OCA], [https://pdbe.org/3zxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zxr RCSB], [https://www.ebi.ac.uk/pdbsum/3zxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zxr ProSAT]</span></td></tr>
</table>
</table>
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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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate--ammonia ligase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Mowbray, S L]]
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[[Category: Mowbray SL]]
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[[Category: Nilsson, M T]]
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[[Category: Nilsson MT]]
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[[Category: Glna1]]
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[[Category: Ligase]]
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[[Category: Mt2278]]
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[[Category: Nucleotide-binding]]
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[[Category: Rv2220]]
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[[Category: Taut state]]
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Current revision

Crystal structure of Mycobacterium Tuberculosis Glutamine Synthetase in complex with tri-substituted imidazole inhibitor (3-(2-tert-butyl- 5-(pyridin-4-yl)-1H-imidazol-4-yl)quinoline) and L-methionine-S- sulfoximine phosphate.

PDB ID 3zxr

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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