6agy: Difference between revisions
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The | ==Aspergillus fumigatus Af293 NDK== | ||
<StructureSection load='6agy' size='340' side='right'caption='[[6agy]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6agy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGY FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </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=6agy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agy OCA], [http://pdbe.org/6agy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6agy RCSB], [http://www.ebi.ac.uk/pdbsum/6agy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6agy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NDK_ASPFU NDK_ASPFU]] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aspergillus fumigatus is a major pathogen of invasive pulmonary aspergillosis with high mortality rate. The nucleoside diphosphate kinase of A. fumigatus, AfNDK (also called SwoH) is essential for its viability, however, its structural characteristic was unknown. In this study, we solved the crystal structure of AfNDK and found that it exists predominantly in form of tetramer in solution. Oligomeric form rather than dimeric form was essential for its kinase activity. The Arg30 and the C terminal amino acids were crucial for dimer-dimer interaction and the viability of A. fumigatus. Mutation V83F might make the secondary structure alpha5 helix protrude outward so that the whole protein structure became unstable at higher temperature, which might subsequently result to the inviability of A. fumigatus under 44 degrees C. In conclusion, the crystal structure of AfNDK was for the first time analyzed and the stability of the tetrameric form with dimer-dimer interaction were crucial for its function in A. fumigatus. | |||
Characterization of crystal structure and key residues of Aspergillus fumigatus nucleoside diphosphate kinase.,Hu Y, Jia X, Lu Z, Han L Biochem Biophys Res Commun. 2019 Mar 26;511(1):148-153. doi:, 10.1016/j.bbrc.2019.01.126. Epub 2019 Feb 14. PMID:30773256<ref>PMID:30773256</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6agy" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nucleoside-diphosphate kinase]] | |||
[[Category: Han, L]] | [[Category: Han, L]] | ||
[[Category: Hu, Y]] | [[Category: Hu, Y]] | ||
[[Category: Kinase]] | |||
[[Category: Transferase]] | |||
Revision as of 14:54, 13 March 2019
Aspergillus fumigatus Af293 NDKAspergillus fumigatus Af293 NDK
Structural highlights
Function[NDK_ASPFU] Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Publication Abstract from PubMedAspergillus fumigatus is a major pathogen of invasive pulmonary aspergillosis with high mortality rate. The nucleoside diphosphate kinase of A. fumigatus, AfNDK (also called SwoH) is essential for its viability, however, its structural characteristic was unknown. In this study, we solved the crystal structure of AfNDK and found that it exists predominantly in form of tetramer in solution. Oligomeric form rather than dimeric form was essential for its kinase activity. The Arg30 and the C terminal amino acids were crucial for dimer-dimer interaction and the viability of A. fumigatus. Mutation V83F might make the secondary structure alpha5 helix protrude outward so that the whole protein structure became unstable at higher temperature, which might subsequently result to the inviability of A. fumigatus under 44 degrees C. In conclusion, the crystal structure of AfNDK was for the first time analyzed and the stability of the tetrameric form with dimer-dimer interaction were crucial for its function in A. fumigatus. Characterization of crystal structure and key residues of Aspergillus fumigatus nucleoside diphosphate kinase.,Hu Y, Jia X, Lu Z, Han L Biochem Biophys Res Commun. 2019 Mar 26;511(1):148-153. doi:, 10.1016/j.bbrc.2019.01.126. Epub 2019 Feb 14. PMID:30773256[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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