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1b0u

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Revision as of 08:30, 25 December 2014

ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM

Structural highlights

1b0u is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HISP_SALTY] Part of the binding-protein-dependent transport system for histidine. Probably responsible for energy coupling to the transport system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety of compounds across membranes of both prokaryotes and eukaryotes. The recently completed Escherichia coli genome sequence revealed that the largest family of paralogous E. coli proteins is composed of ABC transporters. Many eukaryotic proteins of medical significance belong to this family, such as the cystic fibrosis transmembrane conductance regulator (CFTR), the P-glycoprotein (or multidrug-resistance protein) and the heterodimeric transporter associated with antigen processing (Tap1-Tap2). Here we report the crystal structure at 1.5 A resolution of HisP, the ATP-binding subunit of the histidine permease, which is an ABC transporter from Salmonella typhimurium. We correlate the details of this structure with the biochemical, genetic and biophysical properties of the wild-type and several mutant HisP proteins. The structure provides a basis for understanding properties of ABC transporters and of defective CFTR proteins.

Crystal structure of the ATP-binding subunit of an ABC transporter.,Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH Nature. 1998 Dec 17;396(6712):703-7. PMID:9872322^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 1998 Dec 17;396(6712):703-7. PMID:9872322 doi:10.1038/25393

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b0u"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b0u RCSB], [http://www.ebi.ac.uk/pdbsum/1b0u PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HISP_SALTY HISP_SALTY]] Part of the binding-protein-dependent transport system for histidine. Probably responsible for energy coupling to the transport system.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1b0u

From Proteopedia

Revision as of 08:30, 25 December 2014

ATP-BINDING SUBUNIT OF THE HISTIDINE PERMEASE FROM SALMONELLA TYPHIMURIUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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