Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein

Previous characterization of hemophores from Serratia marcescens (HasAs), Pseudomonas aeruginosa (HasAp), and Yersinia pestis (HasAyp) showed that hemin binds between two loops, where it is axially coordinated by H32 and Y75. The Y75 loop is structurally conserved in all three hemophores and harbors...

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Veröffentlicht in:	Biochemistry (Easton) 2016-05, Vol.55 (18), p.2622-2631
Hauptverfasser:	Kumar, Ritesh, Qi, Yifei, Matsumura, Hirotoshi, Lovell, Scott, Yao, Huili, Battaile, Kevin P, Im, Wonpil, Moënne-Loccoz, Pierre, Rivera, Mario
Format:	Artikel
Sprache:	eng
Schlagworte:	absorption alanine Alanine - chemistry Alanine - genetics Alanine - metabolism Amino Acid Substitution Apoproteins - chemistry Apoproteins - genetics Apoproteins - metabolism arginine Arginine - chemistry Arginine - genetics Arginine - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism BASIC BIOLOGICAL SCIENCES Bioinorganic chemistry Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Chemical structure Conformation Crystal structure Electron density heme Heme - chemistry Heme - genetics Heme - metabolism heme iron hydrophobicity Iron - chemistry Iron - metabolism molecular dynamics Molecular Dynamics Simulation Mutation, Missense nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular Protein Structure, Secondary Pseudomonas aeruginosa Pseudomonas aeruginosa - chemistry Pseudomonas aeruginosa - genetics Pseudomonas aeruginosa - metabolism Serratia marcescens X-ray diffraction Yersinia pestis
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