Cupredoxin-like domains in haemocyanins

Jaenicke, Elmar; Büchler, Kay; Markl, Jürgen; Decker, Heinz; Barends, Thomas R. M.

doi:10.1042/bj20091501

Cited by 29 publications

(46 citation statements)

References 45 publications

(64 reference statements)

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“…The central domain (KLH1-h-D2) is equivalent to the Cterminal domain of other FUs (FU-a to FU-g) and contains a bsandwich as its main structural element. The additional C-terminal extension of KLH1-h-D3 folds into one distinct domain with a very high structural similarity to cupredoxins (6). The closest structural neighbor for KLH1-h-D3 identified by submitting the C a -trace to the DALI server is cucumber basic protein.…”

Section: Introductionmentioning

confidence: 99%

“…As type 3 copper proteins and their active sites are embedded in a four a-helix bundle with six histidine residues, which coordinate two copper atoms (4)(5)(6)(7)(8). Between them one molecule oxygen is reversibly bound in side-on (l-g 2 :g 2 ) coordination (4,7,9,10).…”

Section: Introductionmentioning

confidence: 99%

“…Crystal structures of molluscan hemocyanin FUs representing different topological positions in the quaternary structure (wall, inner collar, outer collar) are available (4)(5)(6)(7)(8). The standard molluscan hemocyanin FU (FU-a to FU-f) folds into two domains.…”

Section: Introductionmentioning

confidence: 99%

“…The sequence of this extension could not be related to any other sequence or fold in the databases for a long time. Recently, we reported the structure of keyhole limpet hemocyanin (KLH1-h), which is FU-h of isoform 1 of keyhole limpet (Megathura crenulata) hemocyanin, at 4.0 Å resolution as a C a -trace (6). KLH is a widely used immunological tool (22).…”

Section: Introductionmentioning

confidence: 99%

“…However, KLH1-h-D3 lacks all residues, which form the type-1 active site in cupredoxins. Thus, owing to its similar fold but lack of the active site, the C-terminal domain of KLH1-h was named ''cupredoxin-like domain'' (6).…”

Section: Introductionmentioning

confidence: 99%

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The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

et al. 2011

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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 Cα‐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. © 2011 IUBMB IUBMB Life, 63(3): 183–187, 2011

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

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Structures, Functions, and Assembly of Tyrosinases and Hemocyanins

Fujieda

Itoh

2017

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Metal‐assembling processes in the metalloproteins and metalloenzymes have attracted much recent attention due to their strong relevance not only to enzymology but also to medical science. Concerning the coupled dinuclear copper proteins, so‐called type‐3 copper proteins, a growing amount of information has been accumulated during the past decades. In this chapter, we introduce how copper ions are sorted and transferred to the type‐3 copper proteins in prokaryotic as well as eukaryotic cells. Furthermore, the detailed molecular mechanisms of copper incorporation processes in the type‐3 copper protein active sites will be depicted especially in the bacterial and fungal tyrosinases.

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Cellular and Biomolecular Recognition: Synthetic and non‐Biological Molecules. Edited by Raz Jelinek.

Thomas¹

2010

ChemBioChem

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review the use of immobilized ligands for proteomic applications (affinity chromatography, chemical microarrays), including an excellent compilation of case studies in which the successful identification of the protein target of a bioactive small molecule illuminated the underlying biology. This chapter also provides numerous examples for reactive proteomics. A more in-depth coverage of this blossoming field, sometimes also called activity-based protein profiling, would have been well within the scope of this book.Four more specialized chapters highlight selected applications of small molecule-protein interactions, including an excellent review on fluorescent probes for the in vivo detection of metabolites. Chapter 8 covers the medicinal chemistry of nuclear hormone receptor ligands and their successful translation into the clinic. Chapter 9 emphasizes the impact of small-molecule inhibitors on the understanding of cell motility. Chapter 10 outlines the metabolic engineering of glycoproteins and their subsequent modification with small-molecule probes.The individual chapters are generally well structured and well supported by references for further reading. The quality of the graphics is adequate, with additional colour figures where necessary. Since most chapters present more advanced techniques and/or specialized applications in chemical biology, a sound background in organic chemistry and biochemistry is absolutely required. Given the sheer breadth and diversity of topics that have developed at the interface between chemistry and biology in the past decade, Protein Targeting with Small Molecules does not claim to cover all aspects of chemical biology.Rather, it provides a concise and focused overview centred on how to address small molecule-protein interactions.As such, the book is well suited for advanced graduate students already dedicated to the field or for researchers from related disciplines who want to expand their background at the interface between chemistry and biology. It will be especially valuable to scientists with an interest in translational research and in the prospects of chemical biology towards drug discovery.

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Cupredoxin-like domains in haemocyanins

Cited by 29 publications

References 45 publications

The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

The refined structure of functional unit h of keyhole limpet hemocyanin (KLH1‐h) reveals disulfide bridges

Structures, Functions, and Assembly of Tyrosinases and Hemocyanins

Cellular and Biomolecular Recognition: Synthetic and non‐Biological Molecules. Edited by Raz Jelinek.

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