| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-115 |
Sentence |
denotes |
A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c. |
| T1 |
0-115 |
Sentence |
denotes |
A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c. |
| TextSentencer_T2 |
116-299 |
Sentence |
denotes |
CcmH (cytochromes c maturation protein H) is an essential component of the assembly line necessary for the maturation of c-type cytochromes in the periplasm of Gram-negative bacteria. |
| T2 |
116-299 |
Sentence |
denotes |
CcmH (cytochromes c maturation protein H) is an essential component of the assembly line necessary for the maturation of c-type cytochromes in the periplasm of Gram-negative bacteria. |
| TextSentencer_T3 |
300-495 |
Sentence |
denotes |
The protein is a membrane-anchored thiol-oxidoreductase that has been hypothesized to be involved in the recognition and reduction of apocytochrome c, a prerequisite for covalent heme attachment. |
| T3 |
300-495 |
Sentence |
denotes |
The protein is a membrane-anchored thiol-oxidoreductase that has been hypothesized to be involved in the recognition and reduction of apocytochrome c, a prerequisite for covalent heme attachment. |
| TextSentencer_T4 |
496-648 |
Sentence |
denotes |
Here, we present the 1.7A crystal structure of the soluble periplasmic domain of CcmH from the opportunistic pathogen Pseudomonas aeruginosa (Pa-CcmH*). |
| T4 |
496-648 |
Sentence |
denotes |
Here, we present the 1.7A crystal structure of the soluble periplasmic domain of CcmH from the opportunistic pathogen Pseudomonas aeruginosa (Pa-CcmH*). |
| TextSentencer_T5 |
649-783 |
Sentence |
denotes |
The protein contains a three-helix bundle, i.e. a fold that is different from that of all other thiol-oxidoreductases reported so far. |
| T5 |
649-783 |
Sentence |
denotes |
The protein contains a three-helix bundle, i.e. a fold that is different from that of all other thiol-oxidoreductases reported so far. |
| TextSentencer_T6 |
784-966 |
Sentence |
denotes |
The catalytic Cys residues of the conserved LRCXXC motif (Cys(25) and Cys(28)), located in a long loop connecting the first two helices, form a disulfide bond in the oxidized enzyme. |
| T6 |
784-966 |
Sentence |
denotes |
The catalytic Cys residues of the conserved LRCXXC motif (Cys(25) and Cys(28)), located in a long loop connecting the first two helices, form a disulfide bond in the oxidized enzyme. |
| TextSentencer_T7 |
967-1153 |
Sentence |
denotes |
We have determined the pK(a) values of these 2 Cys residues of Pa-CcmH* (both >8) and propose a possible mechanistic role for a conserved Ser(36) and a water molecule in the active site. |
| T7 |
967-1153 |
Sentence |
denotes |
We have determined the pK(a) values of these 2 Cys residues of Pa-CcmH* (both >8) and propose a possible mechanistic role for a conserved Ser(36) and a water molecule in the active site. |
| TextSentencer_T8 |
1154-1465 |
Sentence |
denotes |
The interaction between Pa-CcmH* and Pa-apocyt c(551) (where cyt c(551) represents cytochrome c(551)) was characterized in vitro following the binding kinetics by stopped-flow using a Trp-containing fluorescent variant of Pa-CcmH* and a dansylated peptide, mimicking the apocytochrome c(551) heme binding motif. |
| T8 |
1154-1465 |
Sentence |
denotes |
The interaction between Pa-CcmH* and Pa-apocyt c(551) (where cyt c(551) represents cytochrome c(551)) was characterized in vitro following the binding kinetics by stopped-flow using a Trp-containing fluorescent variant of Pa-CcmH* and a dansylated peptide, mimicking the apocytochrome c(551) heme binding motif. |
| TextSentencer_T9 |
1466-1676 |
Sentence |
denotes |
The kinetic results show that the protein has a moderate affinity to its apocyt substrate, consistent with the role of Pa-CcmH as an intermediate component of the assembly line for c-type cytochrome biogenesis. |
| T9 |
1466-1676 |
Sentence |
denotes |
The kinetic results show that the protein has a moderate affinity to its apocyt substrate, consistent with the role of Pa-CcmH as an intermediate component of the assembly line for c-type cytochrome biogenesis. |