5luh: Difference between revisions

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'''Unreleased structure'''


The entry 5luh is ON HOLD  until Paper Publication
==AadA E87Q in complex with ATP, calcium and streptomycin==
<StructureSection load='5luh' size='340' side='right' caption='[[5luh]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5luh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SRY:STREPTOMYCIN'>SRY</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5lpa|5lpa]], [[4cs6|4cs6]], [[5g4a|5g4a]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Streptomycin_3''-adenylyltransferase Streptomycin 3''-adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.47 2.7.7.47] </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=5luh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luh OCA], [http://pdbe.org/5luh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5luh RCSB], [http://www.ebi.ac.uk/pdbsum/5luh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5luh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aminoglycoside resistance is commonly conferred by enzymatic modification of drugs by aminoglycoside-modifying enzymes such as aminoglycoside nucleotidyltransferases (ANTs). Here, the first crystal structure of an ANT(3'')(9) adenyltransferase, AadA from Salmonella enterica, is presented. AadA catalyses the magnesium-dependent transfer of adenosine monophosphate from ATP to the two chemically dissimilar drugs streptomycin and spectinomycin. The structure was solved using selenium SAD phasing and refined to 2.5 A resolution. AadA consists of a nucleotidyltransferase domain and an alpha-helical bundle domain. AadA crystallizes as a monomer and is a monomer in solution as confirmed by small-angle X-ray scattering, in contrast to structurally similar homodimeric adenylating enzymes such as kanamycin nucleotidyltransferase. Isothermal titration calorimetry experiments show that ATP binding has to occur before binding of the aminoglycoside substrate, and structure analysis suggests that ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft. Candidate residues for ligand binding and catalysis were subjected to site-directed mutagenesis. In vivo resistance and in vitro binding assays support the role of Glu87 as the catalytic base in adenylation, while Arg192 and Lys205 are shown to be critical for ATP binding.


Authors: Stern, A.L., Van der Verren, S.E., Selmer, M.
Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3'')(9) adenyltransferase.,Chen Y, Nasvall J, Wu S, Andersson DI, Selmer M Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2267-77. doi:, 10.1107/S1399004715016429. Epub 2015 Oct 31. PMID:26527143<ref>PMID:26527143</ref>


Description: AadA E87Q in complex with ATP, calcium and streptomycin
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Stern, A.L]]
<div class="pdbe-citations 5luh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Streptomycin 3''-adenylyltransferase]]
[[Category: Selmer, M]]
[[Category: Selmer, M]]
[[Category: Van Der Verren, S.E]]
[[Category: Stern, A L]]
[[Category: Verren, S E.Van der]]
[[Category: Aminoglycoside adenyl transferase]]
[[Category: Antibiotic resistance]]
[[Category: Transferase]]

Revision as of 09:45, 17 January 2018

AadA E87Q in complex with ATP, calcium and streptomycinAadA E87Q in complex with ATP, calcium and streptomycin

Structural highlights

5luh is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , ,
NonStd Res:,
Activity:-adenylyltransferase Streptomycin 3-adenylyltransferase, with EC number 2.7.7.47
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Aminoglycoside resistance is commonly conferred by enzymatic modification of drugs by aminoglycoside-modifying enzymes such as aminoglycoside nucleotidyltransferases (ANTs). Here, the first crystal structure of an ANT(3)(9) adenyltransferase, AadA from Salmonella enterica, is presented. AadA catalyses the magnesium-dependent transfer of adenosine monophosphate from ATP to the two chemically dissimilar drugs streptomycin and spectinomycin. The structure was solved using selenium SAD phasing and refined to 2.5 A resolution. AadA consists of a nucleotidyltransferase domain and an alpha-helical bundle domain. AadA crystallizes as a monomer and is a monomer in solution as confirmed by small-angle X-ray scattering, in contrast to structurally similar homodimeric adenylating enzymes such as kanamycin nucleotidyltransferase. Isothermal titration calorimetry experiments show that ATP binding has to occur before binding of the aminoglycoside substrate, and structure analysis suggests that ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft. Candidate residues for ligand binding and catalysis were subjected to site-directed mutagenesis. In vivo resistance and in vitro binding assays support the role of Glu87 as the catalytic base in adenylation, while Arg192 and Lys205 are shown to be critical for ATP binding.

Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3)(9) adenyltransferase.,Chen Y, Nasvall J, Wu S, Andersson DI, Selmer M Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2267-77. doi:, 10.1107/S1399004715016429. Epub 2015 Oct 31. PMID:26527143[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Chen Y, Nasvall J, Wu S, Andersson DI, Selmer M. Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3)(9) adenyltransferase. Acta Crystallogr D Biol Crystallogr. 2015 Nov 1;71(Pt 11):2267-77. doi:, 10.1107/S1399004715016429. Epub 2015 Oct 31. PMID:26527143 doi:http://dx.doi.org/10.1107/S1399004715016429

5luh, resolution 1.73Å

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