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000016683 0247_ $$2pmid$$apmid:21445849
000016683 0247_ $$2DOI$$a10.1002/iub.435
000016683 0247_ $$2WOS$$aWOS:000288860900008
000016683 037__ $$aPreJuSER-16683
000016683 041__ $$aeng
000016683 084__ $$2WoS$$aBiochemistry & Molecular Biology
000016683 084__ $$2WoS$$aCell Biology
000016683 1001_ $$0P:(DE-Juel1)VDB101246$$aJaenicke, E.$$b0$$uFZJ
000016683 245__ $$aThe Refined Structure of Functional Unit h of Keyhole Limpet  Hemocyanin (KLH1-h) Reveals Disulfide Bridges
000016683 260__ $$c2011
000016683 300__ $$a183 - 187
000016683 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000016683 520__ $$aHemocyanins are multimeric oxygen-transport proteins in the hemolymph of many arthropods and mollusks. The overall molecular architecture of arthropod and molluscan hemocyanin is very different, although they possess a similar binuclear type 3 copper center to bind oxygen in a side-on conformation. Gastropod hemocyanin is a 35 nm cylindrical didecamer (2 × 10-mer) based on a 400 kDa subunit. The latter is subdivided into eight paralogous "functional units" (FU-a to FU-h), each with an active site. FU-a to FU-f contribute to the cylinder wall, whereas FU-g and FU-h form the internal collar complex. Atomic structures of FU-e and FU-g, and a 9 Å cryoEM structure of the 8 MDa didecamer are available. Recently, the structure of keyhole limpet hemocyanin FU-h (KLH1-h) was presented as a C(α) -trace at 4 Å resolution. Unlike the other seven FU types, FU-h contains an additional C-terminal domain with a cupredoxin-like fold. Because of the resolution limit of 4 Å, in some loops, the course of the protein backbone could not be established with high certainty yet. Here, we present a refined atomic structure of FU-h (KLH1-h) obtained from low-resolution refinement, which unambiguously establishes the course of the polypeptide backbone and reveals the disulfide bridges as well as the orientation of bulky amino acids.
000016683 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000016683 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000016683 588__ $$aDataset connected to Web of Science, Pubmed
000016683 65320 $$2Author$$ahemocyanin
000016683 65320 $$2Author$$acopper protein
000016683 65320 $$2Author$$acupredoxin
000016683 65320 $$2Author$$atype-3 copper
000016683 65320 $$2Author$$amollusca
000016683 65320 $$2Author$$alow-resolution refinement
000016683 650_2 $$2MeSH$$aDisulfides: chemistry
000016683 650_2 $$2MeSH$$aHemocyanin: chemistry
000016683 650_2 $$2MeSH$$aModels, Molecular
000016683 650_7 $$00$$2NLM Chemicals$$aDisulfides
000016683 650_7 $$00$$2NLM Chemicals$$akeyhole-limpet hemocyanin
000016683 650_7 $$09013-72-3$$2NLM Chemicals$$aHemocyanin
000016683 650_7 $$2WoSType$$aJ
000016683 7001_ $$0P:(DE-Juel1)VDB101247$$aBüchler, K.$$b1$$uFZJ
000016683 7001_ $$0P:(DE-Juel1)VDB101248$$aDecker, H$$b2$$uFZJ
000016683 7001_ $$0P:(DE-Juel1)VDB101249$$aMarkl, J.$$b3$$uFZJ
000016683 7001_ $$0P:(DE-Juel1)VDB101250$$aBarends, T.$$b4$$uFZJ
000016683 7001_ $$0P:(DE-Juel1)132018$$aSchröder, G.F.$$b5$$uFZJ
000016683 773__ $$0PERI:(DE-600)2009952-6$$a10.1002/iub.435$$gVol. 63, p. 183 - 187$$p183 - 187$$q63<183 - 187$$tIUBMB Life$$v63$$y2011
000016683 8567_ $$uhttp://dx.doi.org/10.1002/iub.435
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000016683 9141_ $$y2011
000016683 9131_ $$0G:(DE-Juel1)FUEK409$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000016683 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000016683 9132_ $$0G:(DE-HGF)POF3-559H$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vAddenda$$x0
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