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| Hauptseite > Publikationsdatenbank > The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges > print |
| Hauptseite > Publikationsdatenbank > The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges > print |
| 001 | 16683 | ||
| 005 | 20200402210045.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21445849 |
| 024 | 7 | _ | |2 DOI |a 10.1002/iub.435 |
| 024 | 7 | _ | |2 WOS |a WOS:000288860900008 |
| 037 | _ | _ | |a PreJuSER-16683 |
| 041 | _ | _ | |a eng |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Cell Biology |
| 100 | 1 | _ | |0 P:(DE-Juel1)VDB101246 |a Jaenicke, E. |b 0 |u FZJ |
| 245 | _ | _ | |a The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges |
| 260 | _ | _ | |c 2011 |
| 300 | _ | _ | |a 183 - 187 |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |
| 336 | 7 | _ | |2 DataCite |a Output Types/Journal article |
| 336 | 7 | _ | |0 0 |2 EndNote |a Journal Article |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
| 336 | 7 | _ | |2 ORCID |a JOURNAL_ARTICLE |
| 336 | 7 | _ | |2 DRIVER |a article |
| 440 | _ | 0 | |0 24621 |a IUBMB Life |v 63 |y 3 |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK409 |2 G:(DE-HGF) |a Funktion und Dysfunktion des Nervensystems |c P33 |x 0 |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Disulfides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Hemocyanin: chemistry |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Disulfides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a keyhole-limpet hemocyanin |
| 650 | _ | 7 | |0 9013-72-3 |2 NLM Chemicals |a Hemocyanin |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a hemocyanin |
| 653 | 2 | 0 | |2 Author |a copper protein |
| 653 | 2 | 0 | |2 Author |a cupredoxin |
| 653 | 2 | 0 | |2 Author |a type-3 copper |
| 653 | 2 | 0 | |2 Author |a mollusca |
| 653 | 2 | 0 | |2 Author |a low-resolution refinement |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB101247 |a Büchler, K. |b 1 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB101248 |a Decker, H |b 2 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB101249 |a Markl, J. |b 3 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB101250 |a Barends, T. |b 4 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132018 |a Schröder, G.F. |b 5 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)2009952-6 |a 10.1002/iub.435 |g Vol. 63, p. 183 - 187 |p 183 - 187 |q 63<183 - 187 |t IUBMB Life |v 63 |y 2011 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1002/iub.435 |
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| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
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