Mutational analysis eliminates Glu64 and Glu94 as candidates for 'catalytic carboxylate' in the bacterial ATP-binding-cassette protein MalK. (Q38343406)

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scientific article published on August 1997

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English	Mutational analysis eliminates Glu64 and Glu94 as candidates for 'catalytic carboxylate' in the bacterial ATP-binding-cassette protein MalK.	scientific article published on August 1997

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

Mutational analysis eliminates Glu64 and Glu94 as candidates for 'catalytic carboxylate' in the bacterial ATP-binding-cassette protein MalK. (English)

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Europe PubMed Central

PubMed publication ID

2 September 2017

mutational analysis

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based on heuristic

inferred from title

author name string

Stein A

1

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PubMed publication ID

2 September 2017

Hunke S

2

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2 September 2017

Schneider E

3

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2 September 2017

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publication date

1 August 1997

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2 September 2017

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2 September 2017

413

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2 September 2017

2

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2 September 2017

211-214

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Europe PubMed Central

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2 September 2017

ABC Transporters: From Microorganisms to Man

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Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli

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The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations

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A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as

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based on heuristic

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

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Identifiers

10.1016/S0014-5793(97)00913-7

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Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

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