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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1995-2-16
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pubmed:abstractText |
The extracellular siderophore from Mycobacterium smegmatis, exochelin MS, was isolated from iron-deficiently grown cultures and purified to > 98% by a combination of ion-exchange chromatography and h.p.l.c. The material is unextractable into organic solvents, is basic (pI = 9.3-9.5), has a lambda max at 420 nm and a probable Ks for Fe3+ of between 10(25) and 10(30). Its structure has been determined by examination of desferri- and ferri-exochelin and its gallium complex. The methods used were electrospray-m.s. and one- and two-dimensional (NOESY, DQF-COSY and TOCSY) 1H n.m.r. The constituent amino acids were examined by chiral g.l.c analysis of N-trifluoroacetyl isopropyl and N-pentafluoropropionyl methyl esters after hydrolysis, and reductive HI hydrolysis, of the siderophore. The exochelin is a formylated pentapeptide: N-(delta-N-formyl,delta N-hydroxy-R-ornithyl) -beta-alaninyl-delta N-hydroxy-R-ornithinyl-R-allo-threoninyl-delta N-hydroxy-S-ornithine. The linkages involving the three ornithine residues are via their delta N(OH) and alpha-CO groups leaving three free alpha-NH2 groups. Although there are two peptide bonds, these involve the three R (D)-amino acids. Thus the molecule has no conventional peptide bond, and this suggests that it will be resistant to peptidase hydrolysis. The co-ordination centre with Fe3+ is hexadenate in an octahedral structure involving the three hydroxamic acid groups. Molecular modelling shows it to have similar features to other ferric trihydroxamate siderophores whose three-dimensional structures have been established. The molecule is shown to have little flexibility around the iron chelation centre, although the terminal (Orn-3) residue, which is not involved in iron binding except at its delta N atom, has more motional freedom.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-1107222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-2202378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-240908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-2714285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-2942636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-2968361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-3141575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-3309144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-430028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-4425672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-4652567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-4918634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-6826517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-6989958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7826328-7689374
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0264-6021
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
305 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
187-96
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7826328-Amino Acid Sequence,
pubmed-meshheading:7826328-Magnetic Resonance Spectroscopy,
pubmed-meshheading:7826328-Mass Spectrometry,
pubmed-meshheading:7826328-Molecular Sequence Data,
pubmed-meshheading:7826328-Mycobacterium,
pubmed-meshheading:7826328-Peptides, Cyclic,
pubmed-meshheading:7826328-Protein Conformation,
pubmed-meshheading:7826328-Siderophores,
pubmed-meshheading:7826328-Spectrophotometry, Ultraviolet,
pubmed-meshheading:7826328-Stereoisomerism
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pubmed:year |
1995
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pubmed:articleTitle |
Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis.
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pubmed:affiliation |
Department of Chemistry, Cambridge University, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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