6nti

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Current revision (14:49, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6nti' size='340' side='right'caption='[[6nti]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='6nti' size='340' side='right'caption='[[6nti]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nti]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/9entr 9entr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NTI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NTI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nti]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteriaceae Enterobacteriaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NTI 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=9CS:(1R,2S,3S,4R,6S)-4,6-DIAMINO-3-[(3-AMINO-3-DEOXY-ALPHA-D-GLUCOPYRANOSYL)OXY]-2-HYDROXYCYCLOHEXYL+2,6-DIAMINO-2,6-DIDEOXY-ALPHA-D-GLUCOPYRANOSIDE'>9CS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aacC, aac3-VI, aac3-VI_1, NCTC13462_00209, pAPEC1990_61_126, pAR060302_0140, pAR060302_133, peH4H_0115, SAMEA3485113_05325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=543 9ENTR])</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=9CS:(1R,2S,3S,4R,6S)-4,6-DIAMINO-3-[(3-AMINO-3-DEOXY-ALPHA-D-GLUCOPYRANOSYL)OXY]-2-HYDROXYCYCLOHEXYL+2,6-DIAMINO-2,6-DIDEOXY-ALPHA-D-GLUCOPYRANOSIDE'>9CS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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/Aminoglycoside_N(3')-acetyltransferase Aminoglycoside N(3')-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.81 2.3.1.81] </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=6nti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nti OCA], [https://pdbe.org/6nti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nti RCSB], [https://www.ebi.ac.uk/pdbsum/6nti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nti 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=6nti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nti OCA], [http://pdbe.org/6nti PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nti RCSB], [http://www.ebi.ac.uk/pdbsum/6nti PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nti ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C4NV15_ECOLX C4NV15_ECOLX]
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The position, bonding and dynamics of hydrogen atoms in the catalytic centers of proteins are essential for catalysis. The role of short hydrogen bonds in catalysis has remained highly debated and led to establishment of several distinctive geometrical arrangements of hydrogen atoms vis-a-vis the heavier donor and acceptor counterparts, that is, low-barrier, single-well or short canonical hydrogen bonds. Here we demonstrate how the position of a hydrogen atom in the catalytic triad of an aminoglycoside inactivating enzyme leads to a thirty-fold increase in catalytic turnover. A low-barrier hydrogen bond is present in the enzyme active site for the substrates that are turned over the best, whereas a canonical hydrogen bond is found with the least preferred substrate. This is the first comparison of these hydrogen bonds involving an identical catalytic network, while directly demonstrating how active site electrostatics adapt to the electronic nature of substrates to tune catalysis.
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Low-Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad.,Kumar P, Agarwal PK, Waddell MB, Mittag T, Serpersu EH, Cuneo MJ Angew Chem Int Ed Engl. 2019 Nov 4;58(45):16260-16266. doi:, 10.1002/anie.201908535. Epub 2019 Sep 24. PMID:31515870<ref>PMID:31515870</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6nti" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enterobacteriaceae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cuneo, M J]]
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[[Category: Cuneo MJ]]
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[[Category: Kumar, P]]
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[[Category: Kumar P]]
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[[Category: Acetyl transferase]]
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[[Category: Neutron]]
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[[Category: Transferase]]
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[[Category: Transferase-antibiotic complex]]
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Current revision

Neutron/X-ray crystal structure of AAC-VIa bound to kanamycin b

PDB ID 6nti

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