[HTML][HTML] The structural basis of transferrin sequestration by transferrin-binding protein B
C Calmettes, J Alcantara, RH Yu… - Nature structural & …, 2012 - nature.com
C Calmettes, J Alcantara, RH Yu, AB Schryvers, TF Moraes
Nature structural & molecular biology, 2012•nature.comNeisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential
element iron from the host glycoprotein transferrin during infection through a surface
transferrin receptor system composed of proteins TbpA and TbpB. Here we present the
crystal structures of TbpB from N. meningitidis in its apo form and in complex with human
transferrin. The structure reveals how TbpB sequesters and initiates iron release from
human transferrin.
element iron from the host glycoprotein transferrin during infection through a surface
transferrin receptor system composed of proteins TbpA and TbpB. Here we present the
crystal structures of TbpB from N. meningitidis in its apo form and in complex with human
transferrin. The structure reveals how TbpB sequesters and initiates iron release from
human transferrin.
Abstract
Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin.
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