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[[Image:1j7u.jpg|left|200px]]


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==Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa AMPPNP Complex==
The line below this paragraph, containing "STRUCTURE_1j7u", creates the "Structure Box" on the page.
<StructureSection load='1j7u' size='340' side='right'caption='[[1j7u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1j7u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J7U FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1j7u| PDB=1j7u |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j7u OCA], [https://pdbe.org/1j7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j7u RCSB], [https://www.ebi.ac.uk/pdbsum/1j7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j7u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KKA3_ENTFL KKA3_ENTFL] Resistance to kanamycin and structurally-related aminoglycosides, including amikacin.
== 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/j7/1j7u_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=1j7u ConSurf].
<div style="clear:both"></div>


'''Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa AMPPNP Complex'''
==See Also==
 
*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
3',5"-Aminoglycoside phosphotransferase type IIIa [APH(3')-IIIa] is a bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics while exhibiting striking homology to eukaryotic protein kinases (ePK). The structures of APH(3')-IIIa in its apoenzyme form and in complex with the nonhydrolyzable ATP analogue AMPPNP were determined to 3.2 and 2.4 A resolution, respectively. Furthermore, refinement of the previously determined ADP complex was completed. The structure of the apoenzyme revealed alternate positioning of a flexible loop (analogous to the P-loop of ePK's), occupying part of the nucleotide-binding pocket of the enzyme. Despite structural similarity to protein kinases, there was no evidence of domain movement associated with nucleotide binding. This rigidity is due to the presence of more extensive interlobe interactions in the APH(3')-IIIa structure than in the ePK's. Differences between the ADP and AMPPNP complexes are confined to the area of the nucleotide-binding pocket. The position of conserved active site residues and magnesium ions remains unchanged, but there are differences in metal coordination between the two nucleotide complexes. Comparison of the di/triphosphate binding site of APH(3')-IIIa with that of ePK's suggests that the reaction mechanism of APH(3")-IIIa and related aminoglycoside kinases will closely resemble that of eukaryotic protein kinases. However, the orientation of the adenine ring in the binding pocket differs between APH(3')-IIIa and the ePK's by a rotation of approximately 40 degrees. This alternate binding mode is likely a conserved feature among aminoglycoside kinases and could be exploited for the structure-based drug design of compounds to combat antibiotic resistance.
 
==About this Structure==
1J7U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7U OCA].
 
==Reference==
Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase., Burk DL, Hon WC, Leung AK, Berghuis AM, Biochemistry. 2001 Jul 31;40(30):8756-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11467935 11467935]
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
[[Category: Kanamycin kinase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Berghuis AM]]
[[Category: Berghuis, A M.]]
[[Category: Burk DL]]
[[Category: Burk, D L.]]
[[Category: Hon WC]]
[[Category: Hon, W C.]]
[[Category: Leung AK-W]]
[[Category: Leung, A K.W.]]
[[Category: Antibiotic resistance]]
[[Category: Atp-binding]]
[[Category: Kinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:53:46 2008''

Latest revision as of 10:49, 3 April 2024

Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa AMPPNP ComplexCrystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa AMPPNP Complex

Structural highlights

1j7u is a 2 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KKA3_ENTFL Resistance to kanamycin and structurally-related aminoglycosides, including amikacin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1j7u, resolution 2.40Å

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