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1j7i

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Revision as of 08:57, 17 January 2018

Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa Apoenzyme

Structural highlights

1j7i is a 1 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1j7l, 1j7u
Activity:	Kanamycin kinase, with EC number 2.7.1.95
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.

Publication Abstract from PubMed

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.

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:11467935^[1]

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

References

↑ Burk DL, Hon WC, Leung AK, Berghuis AM. Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. Biochemistry. 2001 Jul 31;40(30):8756-64. PMID:11467935

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j7i"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa Apoenzyme==
 <StructureSection load='1j7i' size='340' side='right' caption='[[1j7i]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j7l|1j7l]], [[1j7u|1j7u]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Kanamycin_kinase Kanamycin kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.95 2.7.1.95] </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=1j7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j7i OCA], [http://pdbe.org/1j7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j7i RCSB], [http://www.ebi.ac.uk/pdbsum/1j7i 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=1j7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j7i OCA], [http://pdbe.org/1j7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j7i RCSB], [http://www.ebi.ac.uk/pdbsum/1j7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j7i ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/1j7i_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/1j7i_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1j7i

From Proteopedia

Revision as of 08:57, 17 January 2018

Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type IIIa Apoenzyme

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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