Evidence map›Paper›PMID 19781551›Full record

ArticleJournal of molecular biology2009

Residues gating the periplasmic pathway of LacY.

Yonggang Zhou, Yiling Nie, H Ronald Kaback

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018
    Review
  2. Article
  3. Article
  4. Structure of sugar-bound LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The alternating access transport mechanism in LacY.The Journal of membrane biology · 2011
    Review
  13. Article
  14. Article
  15. Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  16. Helix dynamics in LacY: helices II and IV.Journal of molecular biology · 2010
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Yonggang ZhouDepartment of Physiology, University of California, Los Angeles, CA 90095-7327, USA.
Yiling Nie
H Ronald Kaback
University of California, Los Angeles · US

Funding

SPECIALIZED CENTER FOR THE PROTEIN STRUCTURE INITIATIVEU54GM074929 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STAHLBERG, HENNING · 2005 to 2009
$16.6M
NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Structural Basis for Mechanism of Secondary TransportersR01DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2005 to 2013
$3.7M
Structural Basis for Mechanism of Secondary TransportersR56DK069463 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2009 to 2009
$500k
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK069463NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R01 DK069463NIDDK NIH HHS R56 DK051131NIDDK NIH HHS R56 DK069463NIGMS NIH HHS GM074929NIGMS NIH HHS U54 GM074929
6 · The paper itself

Abstract

X-ray crystal structures of LacY (lactose permease of Escherichia coli) exhibit a large cytoplasmic cavity containing the residues involved in sugar binding and H(+) translocation at the apex and a tightly packed side facing the periplasm. However, biochemical and biophysical evidence provide a strong indication that a hydrophilic pathway opens on the external surface of LacY with closing of the cytoplasmic side upon sugar binding. Thus, an alternating-access mechanism in which sugar- and H(+)-binding sites at the approximate middle of the molecule are alternatively exposed to either side of the membrane is likely to underlie LacY-catalyzed sugar/H(+) symport. To further investigate periplasmic opening, we replaced paired residues on the tightly packed periplasmic side of LacY with Cys, and the effect of cross-linking was studied by testing the accessibility/reactivity of Cys148 with the elongated ( approximately 29 A), impermeant hydrophilic reagent maleimide-PEG2-biotin. When the paired-Cys mutant Ile40-->Cys/Asn245-->Cys containing native Cys148 is oxidized to form a disulfide bond, the reactivity of Cys148 is markedly inhibited. Moreover, the reactivity of Cys148 in this mutant increases with the length of the cross-linking agent. In contrast, maleimide-PEG2-biotin reactivity of Cys148 is unaffected by oxidation of two other paired-Cys mutants at the mouth of the periplasmic cavity. The data indicate that residues Ile40 and Asn245 play a primary role in gating the periplasmic cavity and provide further support for the alternating-access model.

Indexed as

CatalysisCross-Linking ReagentsCrystallography, X-RayCysteineEscherichia coliEscherichia coli ProteinsLactoseMonosaccharide Transport ProteinsMutationPeriplasmProtein ConformationSymportersCross-Linking ReagentsCysteineEscherichia coli ProteinsLactoseLacY protein, E coliMonosaccharide Transport ProteinsSymporters

Identifiers

PMID19781551
PMCPMC2784193
OpenAlexW1995466154

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.