Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis. / Sharma, Neha; Aduri, Nanda G; Iqbal, Anna; Prabhala, Bala K; Mirza, Osman.

In: Journal of Molecular Microbiology and Biotechnology, Vol. 26, No. 5, 2016, p. 312-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sharma, N, Aduri, NG, Iqbal, A, Prabhala, BK & Mirza, O 2016, 'Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis', Journal of Molecular Microbiology and Biotechnology, vol. 26, no. 5, pp. 312-9. https://doi.org/10.1159/000447129

APA

Sharma, N., Aduri, N. G., Iqbal, A., Prabhala, B. K., & Mirza, O. (2016). Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis. Journal of Molecular Microbiology and Biotechnology, 26(5), 312-9. https://doi.org/10.1159/000447129

Vancouver

Sharma N, Aduri NG, Iqbal A, Prabhala BK, Mirza O. Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis. Journal of Molecular Microbiology and Biotechnology. 2016;26(5):312-9. https://doi.org/10.1159/000447129

Author

Sharma, Neha ; Aduri, Nanda G ; Iqbal, Anna ; Prabhala, Bala K ; Mirza, Osman. / Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis. In: Journal of Molecular Microbiology and Biotechnology. 2016 ; Vol. 26, No. 5. pp. 312-9.

Bibtex

@article{b35ca4c433714838a607d1bb351d240b,
title = "Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis",
abstract = "Peptide transport in living organisms is facilitated by either primary transport, hydrolysis of ATP, or secondary transport, cotransport of protons. In this study, we focused on investigating the ligand specificity of the Neisseria meningitidis proton-coupled oligopeptide transporter (NmPOT). It has been shown that the gene encoding this transporter is upregulated during infection. NmPOT conformed to the typical chain length preference as observed in prototypical transporters of this family. In contrast to prototypical transporters, it was unable to accommodate a positively charged peptide residue at the C-terminus position of the substrate peptide. Sequence analysis of the active site of NmPOT displayed a distinctive aromatic patch, which has not been observed in any other transporters from this family. This aromatic patch may be involved in providing NmPOT with its atypical preferences. This study provides important novel information towards understanding how these transporters recognize their substrates.",
keywords = "Journal Article",
author = "Neha Sharma and Aduri, {Nanda G} and Anna Iqbal and Prabhala, {Bala K} and Osman Mirza",
note = "{\textcopyright} 2016 S. Karger AG, Basel.",
year = "2016",
doi = "10.1159/000447129",
language = "English",
volume = "26",
pages = "312--9",
journal = "Journal of Molecular Microbiology and Biotechnology",
issn = "1464-1801",
publisher = "S Karger AG",
number = "5",

}

RIS

TY - JOUR

T1 - Peptide Selectivity of the Proton-Coupled Oligopeptide Transporter from Neisseria meningitidis

AU - Sharma, Neha

AU - Aduri, Nanda G

AU - Iqbal, Anna

AU - Prabhala, Bala K

AU - Mirza, Osman

N1 - © 2016 S. Karger AG, Basel.

PY - 2016

Y1 - 2016

N2 - Peptide transport in living organisms is facilitated by either primary transport, hydrolysis of ATP, or secondary transport, cotransport of protons. In this study, we focused on investigating the ligand specificity of the Neisseria meningitidis proton-coupled oligopeptide transporter (NmPOT). It has been shown that the gene encoding this transporter is upregulated during infection. NmPOT conformed to the typical chain length preference as observed in prototypical transporters of this family. In contrast to prototypical transporters, it was unable to accommodate a positively charged peptide residue at the C-terminus position of the substrate peptide. Sequence analysis of the active site of NmPOT displayed a distinctive aromatic patch, which has not been observed in any other transporters from this family. This aromatic patch may be involved in providing NmPOT with its atypical preferences. This study provides important novel information towards understanding how these transporters recognize their substrates.

AB - Peptide transport in living organisms is facilitated by either primary transport, hydrolysis of ATP, or secondary transport, cotransport of protons. In this study, we focused on investigating the ligand specificity of the Neisseria meningitidis proton-coupled oligopeptide transporter (NmPOT). It has been shown that the gene encoding this transporter is upregulated during infection. NmPOT conformed to the typical chain length preference as observed in prototypical transporters of this family. In contrast to prototypical transporters, it was unable to accommodate a positively charged peptide residue at the C-terminus position of the substrate peptide. Sequence analysis of the active site of NmPOT displayed a distinctive aromatic patch, which has not been observed in any other transporters from this family. This aromatic patch may be involved in providing NmPOT with its atypical preferences. This study provides important novel information towards understanding how these transporters recognize their substrates.

KW - Journal Article

U2 - 10.1159/000447129

DO - 10.1159/000447129

M3 - Journal article

C2 - 27438044

VL - 26

SP - 312

EP - 319

JO - Journal of Molecular Microbiology and Biotechnology

JF - Journal of Molecular Microbiology and Biotechnology

SN - 1464-1801

IS - 5

ER -

ID: 169740283