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==Crystal structure of Seabream Antiquitin and Elucidation of its substrate specificity== | |||
<StructureSection load='2jg7' size='340' side='right'caption='[[2jg7]], [[Resolution|resolution]] 2.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jg7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthopagrus_schlegelii Acanthopagrus schlegelii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JG7 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]] 2.83Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=2jg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jg7 OCA], [https://pdbe.org/2jg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jg7 RCSB], [https://www.ebi.ac.uk/pdbsum/2jg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jg7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4KTQ7_ACASC Q4KTQ7_ACASC] | |||
== 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/jg/2jg7_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=2jg7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8A resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin's specificity towards the substrate alpha-aminoadipic semialdehyde is contributed mainly by Glu120 which interacts with the alpha-amino group of the substrate. On the other hand, Arg300 does not have any specific interaction with the alpha-carboxylate group of the substrate, but is important in maintaining the active site conformation. | |||
The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity.,Tang WK, Wong KB, Lam YM, Cha SS, Cheng CH, Fong WP FEBS Lett. 2008 Sep 3;582(20):3090-6. Epub 2008 Aug 9. PMID:18694748<ref>PMID:18694748</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jg7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]] | *[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Acanthopagrus schlegelii]] | [[Category: Acanthopagrus schlegelii]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cha SS]] | ||
[[Category: | [[Category: Cheng CHK]] | ||
[[Category: | [[Category: Fong WP]] | ||
[[Category: | [[Category: Lee HS]] | ||
[[Category: | [[Category: Tang WK]] | ||
[[Category: | [[Category: Wong KB]] | ||
Latest revision as of 17:46, 13 December 2023
Crystal structure of Seabream Antiquitin and Elucidation of its substrate specificityCrystal structure of Seabream Antiquitin and Elucidation of its substrate specificity
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of seabream antiquitin in complex with the cofactor NAD(+) was solved at 2.8A resolution. The mouth of the substrate-binding pocket is guarded by two conserved residues, Glu120 and Arg300. To test the role of these two residues, we have prepared the two mutants E120A and R300A. Our model and kinetics data suggest that antiquitin's specificity towards the substrate alpha-aminoadipic semialdehyde is contributed mainly by Glu120 which interacts with the alpha-amino group of the substrate. On the other hand, Arg300 does not have any specific interaction with the alpha-carboxylate group of the substrate, but is important in maintaining the active site conformation. The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity.,Tang WK, Wong KB, Lam YM, Cha SS, Cheng CH, Fong WP FEBS Lett. 2008 Sep 3;582(20):3090-6. Epub 2008 Aug 9. PMID:18694748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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