Sulfhydryl groups and disulfide bridges in subunit c of Panulirus interruptus hemocyanin

Neuteboom, Ben; Jekel, Peter A.; Hofstra, Robert; Beintema, Jaap J.

doi:10.1016/0167-4838(89)90263-x

Cited by 6 publications

(1 citation statement)

References 12 publications

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“…The Hc from the spiny lobster Panulirus interruptus is of the arthropodan type and exists as single hexamers in its hemolymph. This Hc can bind oxygen co-operatively and consists of 3 subunits termed a, b and c, which differ in their amino acid sequence [4,5]. Subunits a and b are almost identical with 97% sequence identity, whereas subunit c has 59% sequence identity with a or b.…”

Section: Introductionmentioning

confidence: 99%

Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

et al. 1993

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Section: Introductionmentioning

confidence: 99%

Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

et al. 1993

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Comparison of the hemocyanin β‐barrel with other greek key β‐barrels: Possible importance of the “β‐zipper” in protein structure and folding

Hazes

Hól

1992

Proteins

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The Greek key beta-barrel topology is a folding motif observed in many proteins of widespread evolutionary origin. The arthropodan hemocyanins also have such a Greek key beta-barrel, which forms the core of the third domain of this protein. The hemocyanin beta-barrel was found to be structurally very similar to the beta-barrels of the immunoglobulin domains, Cu,Zn-superoxide dismutase and the chromophore carrying antitumor proteins. The structural similarity within this group of protein families is not accompanied by an evolutionary or functional relationship. It is therefore possible to study structure-sequence relations without bias from nonstructural constraints. The present study reports a conserved pattern of features in these Greek key beta-barrels that is strongly suggestive of a folding nucleation site. This proposed nucleation site, which we call a "beta-zipper," shows a pattern of well-conserved, large hydrophobic residues on two sequential beta-strands joined by a short loop. Each beta-zipper strand is near the center of one of the beta-sheets, so that the two strands face each other from opposite sides of the barrel and interact through their hydrophobic side chains, rather than forming a hydrogen-bonded beta-hairpin. Other protein families with Greek key beta-barrels that do not as strongly resemble the immunoglobulin fold--such as the azurins, plastocyanins, crystallins, and prealbumins--also contain the beta-zipper pattern, which might therefore be a universal feature of Greek key beta-barrel proteins.

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Kinetics of the equilibration of 02 with Panulirus interruptus hemocyanin subunits a, b and c

Cr¹,

Kp²,

Ag³

1993

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Sulfhydryl groups and disulfide bridges in subunit c of Panulirus interruptus hemocyanin

Cited by 6 publications

References 12 publications

Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

Comparative electron microscopy and image analysis of oxy- and deoxy-hemocyanin from the spiny lobster Panulirus interruptus

Comparison of the hemocyanin β‐barrel with other greek key β‐barrels: Possible importance of the “β‐zipper” in protein structure and folding

Kinetics of the equilibration of 02 with Panulirus interruptus hemocyanin subunits a, b and c

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