Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution

Huber, Robert; Schneider, Monika; Mayr, Irmgard; Müller, R.; Deutzmann, Rainer; Suter, Franz; Zuber, Herbert; Falk, Heinz; Kayser, Hartmut

doi:10.1016/0022-2836(87)90296-8

Cited by 230 publications

(172 citation statements)

References 41 publications

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“…Third place is occupied by common SARF from poliovirus (2plv) and tomato bushy stunt virus (2tbv). The similarity in these top 3 cases has already been discussed in the literature (Lebioda & Stec, 1988;Huber et al, 1987;Hogle et al, 1985).…”

Section: Common Sarfssupporting

confidence: 65%

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1994

Protein Science

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We have completed an exhaustive search for the common spatial arrangements of backbone fragments (SARFs) in nonhomologous proteins. This type of local structural similarity, incorporating short fragments of backbone atoms, arranged not necessarily in the same order along the polypeptide chain, appears to be important for protein function and stability. To estimate the statistical significance of the similarities, we have introduced a similarity score. We present several locally similar structures, with a large similarity score, which have not yet been reported. On the basis of the results of pairwise comparison, we have performed hierarchical cluster analysis of protein structures. Our analysis is not limited by comparison of single chains but also includes complex molecules consisting of several subunits. The SARFs with backbone fragments from different polypeptide chains provide a stable interaction between subunits in protein molecules. In many cases the active site of enzymes is located at the same position relative to the common SARFs, implying a function of the certain SARFs as a universal interface of the protein-substrate interaction.

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Section: Common Sarfssupporting

confidence: 65%

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1994

Protein Science

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“…standing of how the family has evolved, suggesting that it is very much older and more widespread than has been supposed. In contrast with their low conservation at the sequence level, analysis of available lipocalin crystal structures, which include plasma retinol-binding protein (RBP) [11], β-lactoglobulin (Blg) [12], insecticyanin [13], bilin-binding protein (BBP) [14,15], major urinary protein (MUP) and α #u -globulin [16], odorant-binding protein (OBP) [17] and epididymal retinoic acid-binding protein [18], shows that the overall folding pattern common to the lipocalins is highly conserved. The nature of this common structure is now well described (see Figures 1 and 2) [2,11].…”

Section: Subunit Molecularmentioning

confidence: 99%

The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,540

1,278

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The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level ; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel β-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily : the calycins. Members of the lipocalin family are characterized by several common molecular-

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“…Sequence comparisons and evolutionary analyses of lipocalins have led to a classification in which 14 clades have been identified [10]. Bacterial lipocalins belong to Clade 1 (the root clade) while the majority of eukaryotic lipocalins ranging from plants to invertebrates and mammals are found in the higher clades (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14).…”

Section: Introductionmentioning

confidence: 99%

“…1) from Escherichia coli, the first bacterial lipocalin that has been identified [2] and whose 3D structure has been solved [11]. The structure of Blc at 1.8 Å resolution revealed a fold similar to that of the moth bilin binding protein (BBP) [12] and the presence of an elongated and open cavity with the proper size to accommodate fatty acids or phospholipids. Blc is an outer-membrane bound protein, facing the periplasmic space.…”

Section: Introductionmentioning

confidence: 99%

The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids

et al. 2006

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Lipocalins, a widespread multifunctional family of small proteins (15-25 kDa) have been first described in eukaryotes and more recently in Gram-negative bacteria. Bacterial lipocalins belonging to class I are outer membrane lipoproteins, among which Blc from E. coli is the better studied. Blc is expressed under conditions of starvation and high osmolarity, conditions known to exert stress on the cell envelope. The structure of Blc that we have previously solved (V. Campanacci, D. Nurizzo, S. Spinelli, C. Valencia, M. Tegoni, C. Cambillau, FEBS Lett. 562 (2004) 183-188.) suggested its possible role in binding fatty acids or phospholipids. Both physiological and structural data on Blc, therefore, point to a role in storage or transport of lipids necessary for membrane maintenance. In order to further document this hypothesis for Blc function, we have performed binding studies using fluorescence quenching experiments. Our results indicate that dimeric Blc binds fatty acids and phospholipids in a micromolar K d range. The crystal structure of Blc with vaccenic acid, an unsaturated C18 fatty acid, reveals that the binding site spans across the Blc dimer, opposite to its membrane anchored face. An exposed unfilled pocket seemingly suited to bind a polar group attached to the fatty acid prompted us to investigate lyso-phospholipids, which were found to bind in a nanomolar K d range. We discuss these findings in terms of a potential role for Blc in the metabolism of lysophospholipids generated in the bacterial outer membrane.

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Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution

Cited by 230 publications

References 41 publications

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The lipocalin protein family: structure and function

The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids

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