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E4PDH catalyzes the first step of the deoxyxylulose\u20105\u2010phosphate (DXP) dependent Vitamin B6 biosynthetic pathway. It utilizes nicotinamide adenine diphosphate (NAD\n                    <jats:sup>+<\/jats:sup>\n                    ) as a co\u2010factor while exhibiting dual catalytic activity wherein it converts (i) D\u2010Erythrose\u20104\u2010phosphate to 4\u2010phosphoerythronate and (ii) Glyceraldehyde\u20103\u2010phosphate to Glyceraldehyde\u20101,3\u2010bisphosphate. An alternate function of\n                    <jats:italic>Ab<\/jats:italic>\n                    E4PDH is the capture of human transferrin (Tf) and lactoferrin (Lf) for bacterial iron acquisition. This study provides the first X\u2010ray crystal structures of\n                    <jats:italic>Ab<\/jats:italic>\n                    E4PDH at a resolution of 2.2\u2009\u00c5. The recombinant enzyme was crystallized under two different conditions with (i) 30% PEG\u2010400 (Crystal\/Structure 1; PDB Id\u20109IIL) and (ii) 1.6\u2009M MgSO\n                    <jats:sub>4<\/jats:sub>\n                    (Crystal\/Structure 2; PDB Id\u20109IIM). The crystal structure reveals a homo\u2010tetramer, with an NAD\n                    <jats:sup>+<\/jats:sup>\n                    bound to each monomer. The structure from Crystal 2 contained only four sulfate ions which were located in the substrate binding sites. In contrast, Crystal 1 showed the presence of several polyethylene glycol (PEG) molecules located in the center of the tetramer contributing to its stability without disturbing co\u2010factor binding. The presence of PEG molecules induced a strong conformational change in the side chain of Gln213, inducing the formation of additional intermolecular contacts and enhancing the stability of the tetramer. Overall, this novel structure has not been observed with other dehydrogenases and may be unique to E4PDH. An insight into this structure would aid in the design of potential small molecule inhibitors to target its biochemical and alternate functions.\n                  <\/jats:p>","DOI":"10.1002\/prot.70083","type":"journal-article","created":{"date-parts":[[2025,11,13]],"date-time":"2025-11-13T10:15:53Z","timestamp":1763028953000},"page":"921-933","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structure of the\n                    <scp>NAD<\/scp>\n                    <sup>+<\/sup>\n                    Bound Erythrose\u20104\u2010Phosphate Dehydrogenase (\n                    <scp>E4PDH<\/scp>\n                    ) Reveals the Stabilizing Effect of Polyethylene Glycol on the Quaternary Structure"],"prefix":"10.1002","volume":"94","author":[{"given":"Viswanathan","family":"Vijayan","sequence":"first","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences  New Delhi India"},{"name":"Department of Biotechnology Faculty of Science and Humanities, SRM Institute of Science and Technology, Kattankulathur Campus  Tamil Nadu India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anjali","family":"Kumari","sequence":"additional","affiliation":[{"name":"Department of Biotechnology National Institute of Pharmaceutical Education and Research  S.A.S. Nagar Punjab India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anamika","family":"Singh","sequence":"additional","affiliation":[{"name":"Department of Biophysics All India Institute of Medical Sciences  New Delhi India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ajay","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biotechnology National Institute of Pharmaceutical Education and Research  S.A.S. 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