TY - JOUR
T1 - Crystallographic structure determination and analysis of a potential short-chain dehydrogenase/reductase (SDR) from multidrug resistant Acinetobacter baumannii
AU - Ghafoori, Seyed Mohammad
AU - Abdollahpour, Soha
AU - Shirmast, Paniz
AU - Forwood, Jade K.
N1 - Publisher Copyright:
© 2023 Ghafoori et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2023/8
Y1 - 2023/8
N2 - Bacterial antibiotic resistance remains an ever-increasing worldwide problem, requiring new approaches and enzyme targets. Acinetobacter baumannii is recognised as one of the most significant antibiotic-resistant bacteria, capable of carrying up to 45 different resistance genes, and new drug discovery targets for this organism is an urgent priority. Short-chain dehydrogenase/reductase enzymes are a large protein family with >60,000 members involved in numerous biosynthesis pathways. Here, we determined the structure of an SDR protein from A. baumannii and assessed the putative co-factor comparisons with previously co-crystalised enzymes and cofactors. This study provides a basis for future studies to examine these potential co-factors in vitro.
AB - Bacterial antibiotic resistance remains an ever-increasing worldwide problem, requiring new approaches and enzyme targets. Acinetobacter baumannii is recognised as one of the most significant antibiotic-resistant bacteria, capable of carrying up to 45 different resistance genes, and new drug discovery targets for this organism is an urgent priority. Short-chain dehydrogenase/reductase enzymes are a large protein family with >60,000 members involved in numerous biosynthesis pathways. Here, we determined the structure of an SDR protein from A. baumannii and assessed the putative co-factor comparisons with previously co-crystalised enzymes and cofactors. This study provides a basis for future studies to examine these potential co-factors in vitro.
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U2 - 10.1371/journal.pone.0289992
DO - 10.1371/journal.pone.0289992
M3 - Article
C2 - 37616198
AN - SCOPUS:85168727176
SN - 1932-6203
VL - 18
SP - 1
EP - 14
JO - PLoS One
JF - PLoS One
IS - 8
M1 - e0289992
ER -