Identical mutations at corresponding positions in two homologous proteins with nonidentical effects

Bjorkman, A.J.; Binnie, R. A.; Cole, L. B.; Zhang, Huide; Hermodson, Mark A.; Mowbray, Sherry L.

doi:10.1016/s0021-9258(19)78110-1

Cited by 10 publications

(3 citation statements)

References 31 publications

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“… The present SAXS/WAXS data can be used for validating the results of the current efforts to use Alphafold2 to predict conformational variants [2 , 3] . The present SAXS/WAXS data, together with available crystal structures of RBP [4] , [5] , [6] , [7] can be used for SAXS/WAXS supported method development efforts [8] , [9] , [10] , [11] , [12] , [13] . Since very few WAXS data sets are available in the public data repositories, the present datasets can aid in method development for accurate calculation of WAXS data from co-ordinates of the structures [14] .…”

Section: Value Of the Datamentioning

confidence: 99%

“…The present SAXS/WAXS data, together with available crystal structures of RBP [4] , [5] , [6] , [7] can be used for SAXS/WAXS supported method development efforts [8] , [9] , [10] , [11] , [12] , [13] .…”

Section: Value Of the Datamentioning

confidence: 99%

“…RBP, which is the periplasmic ribose-binding component of bacterial, ribose-specific ABC transporter, is a two-domain, flexible protein with a hinge adjacent to the sugar binding cleft at the domain interface [4] , [5] , [6] , [7] . A number of crystal structures of RBP have been determined previously in both sugar-bound and free forms [4] , [5] , [6] , [7] ( Fig. 1 ).…”

Section: Data Descriptionmentioning

confidence: 99%

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SAXS/WAXS data of conformationally flexible ribose binding protein

Choudhury,

Yonezawa,

Anu

et al. 2024

Data in Brief

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Section: Value Of the Datamentioning

confidence: 99%

Section: Value Of the Datamentioning

confidence: 99%

Section: Data Descriptionmentioning

confidence: 99%

See 1 more Smart Citation

SAXS/WAXS data of conformationally flexible ribose binding protein

Choudhury,

Yonezawa,

Anu

et al. 2024

Data in Brief

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Modeling of the structure of the Haemophilus influenzae heme‐binding protein suggests a mode of heme interaction

Dunten¹,

Mowbray²

1995

Protein Science

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The structure and function of the periplasmic heme-binding protein HbpA ofHaemophilus influenzae were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide-binding protein of Escherichia coli is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide-binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.Keywords: heme; modeling; periplasmic binding protein; protein structure; transport Haemophilus influenzae is an important cause of meningitis, as well as a major agent of lower respiratory tract and other diseases. The organism has an absolute requirement for exogenously supplied heme, the import of which utilizes a periplasmic lipoprotein, HbpA (Hanson & Hansen, 1991). This heme(haemin)-binding protein is the primary receptor for a heme transport system in the cytoplasmic membrane and, as a key element of the organism's ability to survive in blood, is a desirable target for drugs that would inhibit heme transport. As part of a transport system, it could also be used as a means of selective delivery of toxic compounds into the bacterial cell. The sequence is strongly conserved among various Haemophilus strains (Hanson et al., 1992). A similar protein has also been found in Yersinia enterocolitica (Stojiljkovic & Hantke, 1994) and proposed to exist in Neisseria meningitidis (Stojiljkovic et al., 1995), other hemerequiring pathogens. These facts suggest that drugs aimed at HbpA might be generally useful for a variety of disease-causing bacteria. The success of such a strategy depends largely on the ability to design drugs that do not interfere with the normal roles of heme in the host, and thus also on a knowledge of the modes of heme binding in the protein structures involved. The X-ray Reprint requests to: Sherry L. Mowbray, Department of Molecular Biology, BioMedical Center, Box 590, Swedish University of Agricultural Sciences, 75124 Uppsala, Sweden; e-mail: mowbray@xray.bmc.uu.se.Abbreviations: HbpA, the heme-binding protein of Haemophilus influenzae; DBP, the dipeptide-binding protein of Escherichia coli.

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