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1xef
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1xef |SIZE=350|CAPTION= <scene name='initialview01'>1xef</scene>, resolution 2.50Å | |PDB= 1xef |SIZE=350|CAPTION= <scene name='initialview01'>1xef</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xef OCA], [http://www.ebi.ac.uk/pdbsum/1xef PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xef RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Schmitt, L.]] | [[Category: Schmitt, L.]] | ||
[[Category: Zaitseva, J.]] | [[Category: Zaitseva, J.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: MG]] | ||
[[Category: abc-transporter]] | [[Category: abc-transporter]] | ||
[[Category: atp-dependent transport protein]] | [[Category: atp-dependent transport protein]] | ||
| Line 33: | Line 34: | ||
[[Category: haemolysin b]] | [[Category: haemolysin b]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:48:31 2008'' |
Revision as of 21:48, 30 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the ATP/Mg2+ bound composite dimer of HlyB-NBD
Overview
The ABC transporter HlyB is a central element of the HlyA secretion machinery, a paradigm of Type I secretion. Here, we describe the crystal structure of the HlyB-NBD (nucleotide-binding domain) with H662 replaced by Ala in complex with ATP/Mg2+. The dimer shows a composite architecture, in which two intact ATP molecules are bound at the interface of the Walker A motif and the C-loop, provided by the two monomers. ATPase measurements confirm that H662 is essential for activity. Based on these data, we propose a model in which E631 and H662, highly conserved among ABC transporters, form a catalytic dyad. Here, H662 acts as a 'linchpin', holding together all required parts of a complicated network of interactions between ATP, water molecules, Mg2+, and amino acids both in cis and trans, necessary for intermonomer communication. Based on biochemical experiments, we discuss the hypothesis that substrate-assisted catalysis, rather than general base catalysis might operate in ABC-ATPases.
About this Structure
1XEF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB., Zaitseva J, Jenewein S, Jumpertz T, Holland IB, Schmitt L, EMBO J. 2005 Jun 1;24(11):1901-10. Epub 2005 May 12. PMID:15889153
Page seeded by OCA on Mon Mar 31 00:48:31 2008
