Journal:Acta Cryst F:S2053230X25003905

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<StructureSection load='' size='450' side='right' scene='underdevelopment' caption=''>
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<StructureSection load='' size='450' side='right' scene='10/1080081/015_fig_2a_png/3' caption='Structures of Abmb170h (PDB_ID [[9udy]]). N- and C- terminal regions are colored with blue and red, respectively.'>
===Crystal structure of a recombinant mushroom Agaricus bisporus mannose-binding protein with a longer C-terminal region===
===Crystal structure of a recombinant mushroom Agaricus bisporus mannose-binding protein with a longer C-terminal region===
<big>Dr Hiromi Yoshida</big> <ref>doi: 10.1107/S2053230X25003905</ref>
<big>Dr Hiromi Yoshida</big> <ref>doi: 10.1107/S2053230X25003905</ref>
<hr/>
<hr/>
<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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Agaricus bisporus mannose-binding protein (Abmb, 150 residues) is a ricin B-like type lectin, which has a beta-trefoil fold. Previously reported recombinant C-terminal His-tagged Abmb (additional 12 residues + 6 x His-tag, Abmb168h) showed specific binding activity to mannose and mannitol in surface plasmon resonance analysis. The structure of a recombinant Abmb including additional six residues at the C-terminus after cleavage by TEV protease (Abmb156, PDB code: [[5eha]]) has been reported, however, carbohydrate binding site of Abmb has not yet been determined.
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The present structure of a recombinant Abmb with a longer C-terminal region (14 residues + 6 x His-tag, Abmb170h, crystalized in two forms, orthorhombic (PDB code: [[9udy]]) and monoclinic (PDB code: [[9udz]]) showed high flexibility of several surface loop regions including C-terminal tail. This recombinant Abmb170h did not show binding affinity toward alpha-D-mannose but showed weak binding affinity toward GalNAc and beta-D-galactose in glycan search assay.
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The structure of Abmb170h reveals that the C-terminal region has an impact on the sugar binding and would be important to the mannose binding affinity.
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This can be seen in the comparison of the two Abmb170h structures versus Abmb156.
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* Comparing the structures of <scene name='10/1080081/015_9udy_5eha/5'>Abmb170h Orthorhombic</scene> [[9udy]] vs <scene name='10/1080081/015_9udy_5eha/6'>Abmb156</scene> [[5eha]] we can see plasticity of the C-terminal tail in the <scene name='10/1080081/015_9udy_5eha/7'>animation</scene> <jmol><jmolButton>
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<script>animation off</script>
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</jmolButton>
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</jmol>
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* Comparing the structures <scene name='10/1080081/015_9udza_5eha/7'>Abmb170h Monoclinc (chain A)</scene> [[9udz]] (in which some loops are not seen) vs <scene name='10/1080081/015_9udza_5eha/5'>Abmb156</scene> [[5eha]] we can see plasticity of the C-terminal tail in the <scene name='10/1080081/015_9udza_5eha/6'>animation</scene> <jmol><jmolButton>
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<script>animation off</script>
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</jmolButton>
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</jmol>
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* While comparing the structures of <scene name='10/1080081/015_9udy_9udza/1'>Abmb170h Orthorhombic</scene> [[9udy]] vs <scene name='10/1080081/015_9udy_9udza/5'>Abmb170h Monoclinc (chain A)</scene> [[9udz]] we can see that they look similar in the <scene name='10/1080081/015_9udy_9udza/6'>animation</scene>. <jmol>
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<br>
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This plasticity in the C-terminal tail region could be related to the carbohydrate binding affinity of Abmb.
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<br>
<b>References</b><br>
<b>References</b><br>
<references/>
<references/>
</StructureSection>
</StructureSection>
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Current revision

Structures of Abmb170h (PDB_ID 9udy). N- and C- terminal regions are colored with blue and red, respectively.

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