Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O
Mycobacterium tuberculosis is the causative agent of human tuberculosis, one of the most prevalent infectious diseases in the world. Its genome hosts the glbN and glbO genes coding for two proteins, truncated hemoglobin N (trHbN) and truncated hemoglobin O (trHbO), that belong to different groups (I...
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2008
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| LEADER | 11210caa a22010697a 4500 | ||
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| 001 | PAPER-5616 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203516.0 | ||
| 008 | 190411s2008 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-52249110159 | |
| 024 | 7 | |2 cas |a nitric oxide synthase, 125978-95-2; Bacterial Proteins; GlbN protein, bacteria; Ligands; Mutant Proteins; Truncated Hemoglobins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a PSFGE | ||
| 100 | 1 | |a Boechi, L. | |
| 245 | 1 | 0 | |a Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O |
| 260 | |c 2008 | ||
| 270 | 1 | 0 | |m Estrin, D. A.; Departamento de Quimica Inorganica, Analitica Y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Pabellón II, Buenos Aires (C1428EHA), Argentina; email: dario@qi.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Mycobacterium tuberculosis is the causative agent of human tuberculosis, one of the most prevalent infectious diseases in the world. Its genome hosts the glbN and glbO genes coding for two proteins, truncated hemoglobin N (trHbN) and truncated hemoglobin O (trHbO), that belong to different groups (I and II, respectively) of the recently discovered trHb family of hemeproteins. The different expression pattern and kinetics rates constants for ligand association and NO oxidation rate suggest different functions for these proteins. Previous experimental and theoretical studies showed that, in trHbs, ligand migration along the internal tunnel cavity system is a key issue in determining the ligand-binding characteristics. The X-ray structure of trHbO has been solved and shows several internal cavities and secondary-docking sites. In this work, we present an extensive investigation of the tunnel/cavity system of M. tuberculosis trHbO by means of computer-simulation techniques. We have computed the free-energy profiles for ligand migration along three found tunnels in the oxy and deoxy w.t. and mutant trHbO proteins. Our results show that multiple-ligand migration paths are possible and that several conserved residues such as TrpG8 play a key role in the ligand-migration regulation. © 2008 Wiley-Liss, Inc. |l eng | |
| 593 | |a Departamento de Quimica Inorganica, Analitica Y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Pabellón II, Buenos Aires, Argentina | ||
| 593 | |a Department of Biomolecular Sciences and Biotechnology, CNR-INFM, University of Milano, Milano, Italy | ||
| 593 | |a Department de Fisicoquímica, Institut de Biomedicina, Universitat de Bacelona, Avenida Diagonal, Barcelona, Spain | ||
| 593 | |a Departamento de Quimica Inorganica, Analitica Y Quimica Fisica/INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Pabellón II, Buenos Aires (C1428EHA), Argentina | ||
| 690 | 1 | 0 | |a JARZYNSKI |
| 690 | 1 | 0 | |a LIGAND MIGRATION |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBIN |
| 690 | 1 | 0 | |a HEMOPROTEIN |
| 690 | 1 | 0 | |a NITRIC OXIDE SYNTHASE |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBIN O |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a COMPUTER SIMULATION |
| 690 | 1 | 0 | |a MOLECULAR DYNAMICS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a OXYGEN AFFINITY |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN EXPRESSION |
| 690 | 1 | 0 | |a PROTEIN FUNCTION |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a BACTERIAL PROTEINS |
| 690 | 1 | 0 | |a CRYSTALLOGRAPHY, X-RAY |
| 690 | 1 | 0 | |a LIGANDS |
| 690 | 1 | 0 | |a MUTANT PROTEINS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 690 | 1 | 0 | |a THERMODYNAMICS |
| 690 | 1 | 0 | |a TRUNCATED HEMOGLOBINS |
| 690 | 1 | 0 | |a MYCOBACTERIUM TUBERCULOSIS |
| 700 | 1 | |a Martí, M.A. | |
| 700 | 1 | |a Milani, M. | |
| 700 | 1 | |a Bolognesi, M. | |
| 700 | 1 | |a Luque, F.J. | |
| 700 | 1 | |a Estrin, D.A. | |
| 773 | 0 | |d 2008 |g v. 73 |h pp. 372-379 |k n. 2 |p Proteins Struct. Funct. Genet. |x 08873585 |t Proteins: Structure, Function and Genetics | |
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| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_08873585_v73_n2_p372_Boechi |y Handle |
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