Preliminary time-of-flight neutron diffraction studies of Escherichia coli ABC transport receptor phosphate-binding protein at the Protein Crystallography Station.
(2014) In Acta Crystallographica. Section F: Structural Biology and Crystallization Communications 70(Pt 6). p.819-822- Abstract
- Inorganic phosphate is an essential molecule for all known life. Organisms have developed many mechanisms to ensure an adequate supply, even in low-phosphate conditions. In prokaryotes phosphate transport is instigated by the phosphate-binding protein (PBP), the initial receptor for the ATP-binding cassette (ABC) phosphate transporter. In the crystal structure of the PBP-phosphate complex, the phosphate is completely desolvated and sequestered in a deep cleft and is bound by 13 hydrogen bonds: 12 to protein NH and OH donor groups and one to a carboxylate acceptor group. The carboxylate plays a key recognition role by accepting a phosphate hydrogen. PBP phosphate affinity is relatively consistent across a broad pH range, indicating the... (More)
- Inorganic phosphate is an essential molecule for all known life. Organisms have developed many mechanisms to ensure an adequate supply, even in low-phosphate conditions. In prokaryotes phosphate transport is instigated by the phosphate-binding protein (PBP), the initial receptor for the ATP-binding cassette (ABC) phosphate transporter. In the crystal structure of the PBP-phosphate complex, the phosphate is completely desolvated and sequestered in a deep cleft and is bound by 13 hydrogen bonds: 12 to protein NH and OH donor groups and one to a carboxylate acceptor group. The carboxylate plays a key recognition role by accepting a phosphate hydrogen. PBP phosphate affinity is relatively consistent across a broad pH range, indicating the capacity to bind monobasic (H2PO4(-)) and dibasic (HPO4(2-)) phosphate; however, the mechanism by which it might accommodate the second hydrogen of monobasic phosphate is unclear. To answer this question, neutron diffraction studies were initiated. Large single crystals with a volume of 8 mm(3) were grown and subjected to hydrogen/deuterium exchange. A 2.5 Å resolution data set was collected on the Protein Crystallography Station at the Los Alamos Neutron Science Center. Initial refinement of the neutron data shows significant nuclear density, and refinement is ongoing. This is the first report of a neutron study from this superfamily. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4528942
- author
- Sippel, K H ; Bacik, J ; Quiocho, F A and Fisher, Zoe LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Crystallographica. Section F: Structural Biology and Crystallization Communications
- volume
- 70
- issue
- Pt 6
- pages
- 819 - 822
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:24915101
- wos:000337062500028
- scopus:84905446674
- pmid:24915101
- ISSN
- 2053-230X
- DOI
- 10.1107/S2053230X14009704
- language
- English
- LU publication?
- yes
- id
- cf01adf8-5601-4e87-88f6-ee39843cdf88 (old id 4528942)
- date added to LUP
- 2016-04-01 10:47:43
- date last changed
- 2022-02-02 21:06:32
@article{cf01adf8-5601-4e87-88f6-ee39843cdf88,
abstract = {{Inorganic phosphate is an essential molecule for all known life. Organisms have developed many mechanisms to ensure an adequate supply, even in low-phosphate conditions. In prokaryotes phosphate transport is instigated by the phosphate-binding protein (PBP), the initial receptor for the ATP-binding cassette (ABC) phosphate transporter. In the crystal structure of the PBP-phosphate complex, the phosphate is completely desolvated and sequestered in a deep cleft and is bound by 13 hydrogen bonds: 12 to protein NH and OH donor groups and one to a carboxylate acceptor group. The carboxylate plays a key recognition role by accepting a phosphate hydrogen. PBP phosphate affinity is relatively consistent across a broad pH range, indicating the capacity to bind monobasic (H2PO4(-)) and dibasic (HPO4(2-)) phosphate; however, the mechanism by which it might accommodate the second hydrogen of monobasic phosphate is unclear. To answer this question, neutron diffraction studies were initiated. Large single crystals with a volume of 8 mm(3) were grown and subjected to hydrogen/deuterium exchange. A 2.5 Å resolution data set was collected on the Protein Crystallography Station at the Los Alamos Neutron Science Center. Initial refinement of the neutron data shows significant nuclear density, and refinement is ongoing. This is the first report of a neutron study from this superfamily.}},
author = {{Sippel, K H and Bacik, J and Quiocho, F A and Fisher, Zoe}},
issn = {{2053-230X}},
language = {{eng}},
number = {{Pt 6}},
pages = {{819--822}},
publisher = {{Wiley-Blackwell}},
series = {{Acta Crystallographica. Section F: Structural Biology and Crystallization Communications}},
title = {{Preliminary time-of-flight neutron diffraction studies of Escherichia coli ABC transport receptor phosphate-binding protein at the Protein Crystallography Station.}},
url = {{http://dx.doi.org/10.1107/S2053230X14009704}},
doi = {{10.1107/S2053230X14009704}},
volume = {{70}},
year = {{2014}},
}