Crystal structures of hen egg-white lysozyme complexes with gadolinium(III) and gadolinium(III)-N-acetyl-D-glucosamine.
Identifieur interne : 000133 ( Pmc/Corpus ); précédent : 000132; suivant : 000134Crystal structures of hen egg-white lysozyme complexes with gadolinium(III) and gadolinium(III)-N-acetyl-D-glucosamine.
Auteurs : S J Perkins ; L N Johnson ; P A Machin ; D C PhillipsSource :
- Biochemical Journal [ 0264-6021 ] ; 1979.
Abstract
Analysis at 0.25 nm resolution of the crystal structures of lysozyme-Gd(III) and lysozyme-Gd(III)-N-acetyl-D-glucosamine (GlcNac), prepared by diffusion methods, show that there are two main binding positions for Gd(III), one of which is close to glutamic acid-35 and the other close to aspartic acid-52. The two sites are 0.36 nm part. There is no evidence for the weak binding of Gd(III) to any of the eight other carboxy groups of lysozyme. In the presence of Gd(III), the binding of GlcNac is similar to that observed for the binding of the beta-anomer in subsite C. There are numerous small conformational changes in the protein on binding (Gd(III) and the sugar, and these have been quantified to a first approximation by real-space refinement. These changes are similar in both structures, and involve, among other small movements, shifts of one of the disulphide bridges by up to 0.05 nm. The movement of residues 70--74 observed in the binary complex of lysozyme-GlcNac [Perkins, Johnson, Machin & Phillips (1978) Biochem. J. 173-617] is not observed in the ternary complex of lysozyme-Gd(III)-GlcNac. The nature of the lysozyme-Gd(III) complex is discussed in the light of evidence from other crystallographic studies and n.m.r. solution studies. Preliminary findings for a lysozyme-Gd(III) complex prepared by co-crystallization methods are reported.
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PubMed: 486153
PubMed Central: 1161121
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PMC:1161121Le document en format XML
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<author><name sortKey="Perkins, S J" sort="Perkins, S J" uniqKey="Perkins S" first="S J" last="Perkins">S J Perkins</name>
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<author><name sortKey="Johnson, L N" sort="Johnson, L N" uniqKey="Johnson L" first="L N" last="Johnson">L N Johnson</name>
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<author><name sortKey="Machin, P A" sort="Machin, P A" uniqKey="Machin P" first="P A" last="Machin">P A Machin</name>
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<author><name sortKey="Phillips, D C" sort="Phillips, D C" uniqKey="Phillips D" first="D C" last="Phillips">D C Phillips</name>
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<front><div type="abstract" xml:lang="en"><p>Analysis at 0.25 nm resolution of the crystal structures of lysozyme-Gd(III) and lysozyme-Gd(III)-N-acetyl-D-glucosamine (GlcNac), prepared by diffusion methods, show that there are two main binding positions for Gd(III), one of which is close to glutamic acid-35 and the other close to aspartic acid-52. The two sites are 0.36 nm part. There is no evidence for the weak binding of Gd(III) to any of the eight other carboxy groups of lysozyme. In the presence of Gd(III), the binding of GlcNac is similar to that observed for the binding of the beta-anomer in subsite C. There are numerous small conformational changes in the protein on binding (Gd(III) and the sugar, and these have been quantified to a first approximation by real-space refinement. These changes are similar in both structures, and involve, among other small movements, shifts of one of the disulphide bridges by up to 0.05 nm. The movement of residues 70--74 observed in the binary complex of lysozyme-GlcNac [Perkins, Johnson, Machin & Phillips (1978) Biochem. J. 173-617] is not observed in the ternary complex of lysozyme-Gd(III)-GlcNac. The nature of the lysozyme-Gd(III) complex is discussed in the light of evidence from other crystallographic studies and n.m.r. solution studies. Preliminary findings for a lysozyme-Gd(III) complex prepared by co-crystallization methods are reported.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochem J</journal-id>
<journal-title>Biochemical Journal</journal-title>
<issn pub-type="ppub">0264-6021</issn>
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<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
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<title-group><article-title>Crystal structures of hen egg-white lysozyme complexes with gadolinium(III) and gadolinium(III)-N-acetyl-D-glucosamine.</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Perkins</surname>
<given-names>S J</given-names>
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<contrib contrib-type="author"><name><surname>Johnson</surname>
<given-names>L N</given-names>
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<contrib contrib-type="author"><name><surname>Machin</surname>
<given-names>P A</given-names>
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<contrib contrib-type="author"><name><surname>Phillips</surname>
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<pub-date pub-type="ppub"><day>1</day>
<month>7</month>
<year>1979</year>
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<volume>181</volume>
<issue>1</issue>
<fpage>21</fpage>
<lpage>36</lpage>
<abstract><p>Analysis at 0.25 nm resolution of the crystal structures of lysozyme-Gd(III) and lysozyme-Gd(III)-N-acetyl-D-glucosamine (GlcNac), prepared by diffusion methods, show that there are two main binding positions for Gd(III), one of which is close to glutamic acid-35 and the other close to aspartic acid-52. The two sites are 0.36 nm part. There is no evidence for the weak binding of Gd(III) to any of the eight other carboxy groups of lysozyme. In the presence of Gd(III), the binding of GlcNac is similar to that observed for the binding of the beta-anomer in subsite C. There are numerous small conformational changes in the protein on binding (Gd(III) and the sugar, and these have been quantified to a first approximation by real-space refinement. These changes are similar in both structures, and involve, among other small movements, shifts of one of the disulphide bridges by up to 0.05 nm. The movement of residues 70--74 observed in the binary complex of lysozyme-GlcNac [Perkins, Johnson, Machin & Phillips (1978) Biochem. J. 173-617] is not observed in the ternary complex of lysozyme-Gd(III)-GlcNac. The nature of the lysozyme-Gd(III) complex is discussed in the light of evidence from other crystallographic studies and n.m.r. solution studies. Preliminary findings for a lysozyme-Gd(III) complex prepared by co-crystallization methods are reported.</p>
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