2011
DOI: 10.1016/j.jmb.2011.04.036
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The X-ray Structure of the Zinc Transporter ZnuA from Salmonella enterica Discloses a Unique Triad of Zinc-Coordinating Histidines

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Cited by 39 publications
(49 citation statements)
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“…Whereas the same coordination may be likely assumed also by S. enterica ZnuA [14], the crystal structure of this protein has revealed a distinct metal coordination involving a His residue from the mobile His-loop and it has been suggested that this peculiar metal coordination may be favored by low metal occupancy [11]. These findings suggest that the two metal binding regions may be correlated and that the His-loop may have a direct role in zinc transport, either by facilitating zinc transfer from the His-loop to the primary metal binding site or from ZnuA to ZnuB.…”
Section: Introductionmentioning
confidence: 65%
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“…Whereas the same coordination may be likely assumed also by S. enterica ZnuA [14], the crystal structure of this protein has revealed a distinct metal coordination involving a His residue from the mobile His-loop and it has been suggested that this peculiar metal coordination may be favored by low metal occupancy [11]. These findings suggest that the two metal binding regions may be correlated and that the His-loop may have a direct role in zinc transport, either by facilitating zinc transfer from the His-loop to the primary metal binding site or from ZnuA to ZnuB.…”
Section: Introductionmentioning
confidence: 65%
“…We have chosen to use a model of the S. enterica ZnuA, rather than its available X-ray structure [11], because in that structure, due to its high mobility, the Hisloop is absent with the exception of a short segment containing an histidine coordinating the metal. This particular ligand arrangement [11] may correspond to a ZnuA transient intermediate in which the zinc is transferred from the His-loop to the primary metal binding site, but it is not suitable to explain the results of our fluorescence experiments.…”
Section: Znua Modelingmentioning
confidence: 99%
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