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@ARTICLE{Jaenicke:16683,
      author       = {Jaenicke, E. and Büchler, K. and Decker, H and Markl, J.
                      and Barends, T. and Schröder, G.F.},
      title        = {{T}he {R}efined {S}tructure of {F}unctional {U}nit h of
                      {K}eyhole {L}impet {H}emocyanin ({KLH}1-h) {R}eveals
                      {D}isulfide {B}ridges},
      journal      = {IUBMB Life},
      volume       = {63},
      reportid     = {PreJuSER-16683},
      pages        = {183 - 187},
      year         = {2011},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Hemocyanins are multimeric oxygen-transport proteins in the
                      hemolymph of many arthropods and mollusks. The overall
                      molecular architecture of arthropod and molluscan hemocyanin
                      is very different, although they possess a similar binuclear
                      type 3 copper center to bind oxygen in a side-on
                      conformation. Gastropod hemocyanin is a 35 nm cylindrical
                      didecamer (2 × 10-mer) based on a 400 kDa subunit. The
                      latter is subdivided into eight paralogous "functional
                      units" (FU-a to FU-h), each with an active site. FU-a to
                      FU-f contribute to the cylinder wall, whereas FU-g and FU-h
                      form the internal collar complex. Atomic structures of FU-e
                      and FU-g, and a 9 Å cryoEM structure of the 8 MDa didecamer
                      are available. Recently, the structure of keyhole limpet
                      hemocyanin FU-h (KLH1-h) was presented as a C(α) -trace at
                      4 Å resolution. Unlike the other seven FU types, FU-h
                      contains an additional C-terminal domain with a
                      cupredoxin-like fold. Because of the resolution limit of 4
                      Å, in some loops, the course of the protein backbone could
                      not be established with high certainty yet. Here, we present
                      a refined atomic structure of FU-h (KLH1-h) obtained from
                      low-resolution refinement, which unambiguously establishes
                      the course of the polypeptide backbone and reveals the
                      disulfide bridges as well as the orientation of bulky amino
                      acids.},
      keywords     = {Disulfides: chemistry / Hemocyanin: chemistry / Models,
                      Molecular / Disulfides (NLM Chemicals) / keyhole-limpet
                      hemocyanin (NLM Chemicals) / Hemocyanin (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ICS-6},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21445849},
      UT           = {WOS:000288860900008},
      doi          = {10.1002/iub.435},
      url          = {https://juser.fz-juelich.de/record/16683},
}