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< | ==Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase== | ||
<StructureSection load='1v4a' size='340' side='right'caption='[[1v4a]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V4A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1v4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4a OCA], [https://pdbe.org/1v4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v4a RCSB], [https://www.ebi.ac.uk/pdbsum/1v4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v4a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLNE_ECOLI GLNE_ECOLI] Adenylation and deadenylation of glutamate--ammonia ligase.<ref>PMID:8412694</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v4/1v4a_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1v4a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding. | |||
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.,Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL Structure. 2004 May;12(5):861-9. PMID:15130478<ref>PMID:15130478</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1v4a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Carr | [[Category: Carr PD]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Ollis | [[Category: Ollis DL]] | ||
[[Category: Vasudevan | [[Category: Vasudevan SG]] | ||
[[Category: Xu | [[Category: Xu Y]] | ||
[[Category: Zhang | [[Category: Zhang R]] | ||
Latest revision as of 02:57, 28 December 2023
Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferaseStructure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase
Structural highlights
FunctionGLNE_ECOLI Adenylation and deadenylation of glutamate--ammonia ligase.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.,Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL Structure. 2004 May;12(5):861-9. PMID:15130478[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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