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| - | [[Image:2pmk.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2pmk| PDB=2pmk | SCENE= }} | | {{STRUCTURE_2pmk| PDB=2pmk | SCENE= }} |
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| - | '''Crystal structures of an isolated ABC-ATPase in complex with TNP-ADP'''
| + | ===Crystal structures of an isolated ABC-ATPase in complex with TNP-ADP=== |
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| - | ==Overview==
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| - | TNP-modified nucleotides have been used extensively to study protein-nucleotide interactions. In the case of ABC-ATPases, application of these powerful tools has been greatly restricted due to the significantly higher affinity of the TNP-nucleotide for the corresponding ABC-ATPase in comparison to the non-modified nucleotides. To understand the molecular changes occurring upon binding of the TNP-nucleotide to an ABC-ATPase, we have determined the crystal structure of the TNP-ADP/HlyB-NBD complex at 1.6A resolution. Despite the higher affinity of TNP-ADP, no direct fluorophore-protein interactions were observed. Unexpectedly, only water-mediated interactions were detected between the TNP moiety and Tyr(477), that is engaged in pi-pi stacking with the adenine ring, as well as with two serine residues (Ser(504) and Ser(509)) of the Walker A motif. Interestingly, the side chains of these two serine residues adopt novel conformations that are not observed in the corresponding ADP structure. However, in the crystal structure of the S504A mutant, which binds TNP-ADP with similar affinity to the wild type enzyme, a novel TNP-water interaction compensates for the missing serine side chain. Since this water molecule is not present in the wild type enzyme, these results suggest that only water-mediated interactions provide a structural explanation for the increased affinity of TNP-nucleotides towards ABC-ATPases. However, our results also imply that in silico approaches such as docking or modeling cannot directly be applied to generate 'affinity-adopted' ADP- or ATP-analogs for ABC-ATPases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18155559}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18155559 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18155559}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tnp-nucleotide]] | | [[Category: Tnp-nucleotide]] |
| | [[Category: Transport protein]] | | [[Category: Transport protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:30:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:21:27 2008'' |
Revision as of 01:21, 29 July 2008
Template:STRUCTURE 2pmk
Crystal structures of an isolated ABC-ATPase in complex with TNP-ADP
Template:ABSTRACT PUBMED 18155559
About this Structure
2PMK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Water-mediated protein-fluorophore interactions modulate the affinity of an ABC-ATPase/TNP-ADP complex., Oswald C, Jenewein S, Smits SH, Holland IB, Schmitt L, J Struct Biol. 2007 Nov 21;. PMID:18155559
Page seeded by OCA on Tue Jul 29 04:21:27 2008
