Mycobacterium kansasii 824. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. Gene. Primary publication DOI: 10.1042/BCJ20190827. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. Status. DOI: 10.2210/pdb6q09/pdb. Unreviewed-Annotation score: -Experimental evidence at protein level i. PDB Entry - 6U3L (Status - Released) Summary information: Title: Crystal structure of Hemerythrin HHE cation binding domain-containing protein: Rv2633c homolog from Mycobacterium kansasii DOI: 10.2210/pdb6u3l/pdb Primary publication DOI: 10.1042/BCJ20190827 Entry authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Initial deposition on: 22 August 2019 Entry authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Initial deposition on: 1 August 2019 The HHE cation-binding domain was first predicted by bioinformatics methods as a domain composed of two helical regions and a conserved HHE cation-binding site . Abendroth, J. et al., Crystal structure of zinc-bound Hemerythrin HHE cation binding domain-containing protein (soak): Rv2633c homolog from Mycobacterium kansasii. The hemerythrin-like domain family is a repetition of the HHE cation-binding domain, which folds into an up-and-down bundle of four left-handed helices [14,23]. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. Furthermore, structural data on hemerythrin‐like domains from two proteins of unknown function, PF0695 from Pyrococcus furiosus and NMB1532 from Neisseria meningitidis, show that the cation‐binding sites, typical of hemerythrin, can be absent or be occupied by metal ions other than iron. Title: Crystal structure of iron-bound Hemerythrin HHE cation binding domain-containing protein: Rv2633c homolog from Mycobacterium kansasii. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. The hemerythrin/HHE cation-binding domain occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. Function i Caution. I547_5247. The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. Hemerythrin HHE cation binding domain protein. Organism. Crystal structure of zinc-bound Hemerythrin HHE cation binding domain-containing protein (soak): Rv2633c homolog from Mycobacterium kansasii: Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) R / R free: 0.18 / 0.21: Unit cell edges [Å] hemerythrin-like protein (HL P) with an HHE (histidine-histidine-glutamic acid) cation-binding domain [7]. Phylogenetic analysis indicated that Rv2633c is a member of a distinct subset of hemerythrin-like proteins exclusive to mycobacteria. This domain binds iron in hemerythrin, but can bind other metals in related proteins, such as cadmium in the Nereis diversicolor hemerythrin. Hemerythrins do not contain heme but use non-heme irons for oxygen transport or to be published Release Date 2020-01-22 Peptides Hemerythrin HHE cation binding domain protein: A SMTL:PDB Here, we analyzed the Rv2633c protein sequence, which revealed the presence of an HHE cation-binding domain common in hemerythrin-like proteins. These genes were identified as N-acetyltransferases (two genes), putative carboxylesterase, 3-carboxy-cis,cis-muconate cycloisomerase, hemerythrin HHE cation binding domain protein, 3-hydroxyacyl CoA dehydrogenase, putative F420 dependent oxidase, NAD binding protein 3-hydroxylacyl-CoA dehydrogenase, and a putative uncharacterized protein .

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