Influence of proline residues on protein conformation

MacArthur, Malcolm W.; Thornton, Janet M.

doi:10.1016/0022-2836(91)90721-h

Cited by 1,093 publications

(887 citation statements)

References 29 publications

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“…-~Although prolyl residues are thought to play an important role in the structure and function of many proteins [132], and despite the fact that proline residues are relatively abundant in the transmembrane segments of polytopic membrane proteins [133,134], sitedirected mutagenesis of these residues does not indicate an essential role for the prolines in the lactose carrier protein of E. coli. Neither cis/trans isomerization of the peptide bond preceding proline nor possible structural discontinuities, 'kinks', in the transmembrane a-helical domains due to the presence of proline residues appear to be important for membrane insertion, stability and activity of LacY [135,136].…”

Section: Iv-a Primary Sequence and Secondary Structurementioning

confidence: 99%

Secondary solute transport in bacteria

Poolman

Konings

1993

Biochimica et Biophysica Acta (BBA) - Bioenergetics

202

160

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Section: Iv-a Primary Sequence and Secondary Structurementioning

confidence: 99%

Secondary solute transport in bacteria

Poolman

Konings

1993

Biochimica et Biophysica Acta (BBA) - Bioenergetics

202

160

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“…As was calculated via published methods about 5% of all peptidyl-prolyl bonds known in the spatial structure are in the cis conformation in native proteins [15,16]. The trans to cis isomerization is often the rate limiting step during the refolding of polypeptides provided that there is a cis prolyl residue in the native state [8,17,18].…”

Section: Introductionmentioning

confidence: 99%

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

Stoller¹,

Tradler²,

Rücknagel³

et al. 1996

FEBS Letters

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The 48 kDa trigger factor (TF) of E. coli was shown to be a peptidyl-prolyl cisltrans isomerase (PPIase). Its location on a ribosomal particle is unique among the PPIases described so far, and suggests a role in de novo protein folding. The trigger factor was investigated with regard to a domain carrying the catalytic activity. An enzymatieally active fragment could be isolated after proteolysis by subtifisin. The resulting polypeptide was analysed by N-terminal sequencing and MALDI-TOF mass spectrometry revealing an 11.8 kDa fragment of TF encompassing the amino acid residues Arg-145 to Glu-251. The nucleotide sequence encoding the amino acid residues Met-140 to Ala-250 of the TF was cloned into vector pQE32. After expression in E. coli the resulting His-tagged polypeptide was isolated on an Ni 2+-NTA column. Subsequent digestion with subtifisin and anionexchange chromatography yielded a TF fragment encompassing amino acids Gin-148 to Thr-249. This fragment may represent the catalytic core of TF since PPIase activity with a specificity constant kcat/Km of 1.3 ~1-1 s -l could be demonstrated when using Suc-Ala-Phe-Pro-Phe-NH-Np as a substrate. Moreover, as was observed for the complete, authentic TF the PPIase activity of the fragment was not inhibited by the peptidomacrofide FK506.

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“…Compared to other amino acids, proline also appears more frequently in proteins with a cis peptide bond [3]. Proline residues thus have a special significance in their effect on chain conformation, which in turn can influence protein folding, and also peptide and protein function [4].…”

Section: Introductionmentioning

confidence: 99%

β‐Turns induced in bradykinin by (S)‐α‐methylproline

1992

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The ability of (S).g-methylprolin¢ (g-MePro) to stabilis¢ reversequrn conformations in the peptlde hormone brad~/kinin (BK = Argt-Pro:-ProLGly 4-PheS-Ser6-ProLPhe~-Arg ~) has been investigated. Two BK analogues containing ,)-MePro at position 3 or position 7 were synthesised and their conformations in aqueous solution investigated by NMR spectroscopy. Whereas BK is largely disordered on the NMR time scale both analogues showed ROE connectivities in 2D-ROESY spectra indicative of reverse-turn conformations at both Pro2-Phe ~ and Ser~-Arg °. whose formation appears to be cooperative. Some potential applications of ~z-McPro as a reverse-turn mimetic in the construction of synthetic peptide libraries is discussed.

show abstract

Influence of proline residues on protein conformation

Cited by 1,093 publications

References 29 publications

Secondary solute transport in bacteria

Secondary solute transport in bacteria

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

β‐Turns induced in bradykinin by (S)‐α‐methylproline

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