1v4a: Difference between revisions
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<StructureSection load='1v4a' size='340' side='right' caption='[[1v4a]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1v4a' size='340' side='right' caption='[[1v4a]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v4a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1v4a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V4A FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Glutamate--ammonia-ligase]_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.42 2.7.7.42] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Glutamate--ammonia-ligase]_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.42 2.7.7.42] </span></td></tr> | ||
<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=1v4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1v4a RCSB], [http://www.ebi.ac.uk/pdbsum/1v4a PDBsum]</span></td></tr> | <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=1v4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4a OCA], [http://pdbe.org/1v4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v4a RCSB], [http://www.ebi.ac.uk/pdbsum/1v4a PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1v4a" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Carr, P D]] | [[Category: Carr, P D]] | ||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
Revision as of 03:49, 11 September 2015
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
Function[GLNE_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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