Difference between revisions of "Part:BBa K1640019:Design"
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===Design Notes=== | ===Design Notes=== | ||
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| + | This part is to be combined with GUN4 to form operon-1, one of four operons engineered for synthesis of chlorophyll-biosynthesis pathway. | ||
| + | Magnesium chelatase sits at the branch point of the common tetrapyrrole pathway and inserts Mg2+ into Proto to produce Mg-Proto, the first unique intermediate of the chlorophyll biosynthetic pathway. It is known that the BchH/ChlH subunit binds the substrate and, for this reason, is thought to be the catalytic component of the enzyme. The ChlH subunit makes conformational changes upon binding its porphyrin substrate. | ||
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| + | A study done on ''Rhodobacter capsulatus'' has demonstrated the apo structure to contain three major lobe-shaped domains connected at a single point, with additional densities at the tip of two lobes termed the “thumb” and “finger” (figure: 2). This independent reconstruction of a substrate-bound ChlH complex permitted insight into substrate-induced conformational changes (Sirijovski et al., 2008). | ||
===Source=== | ===Source=== | ||
| − | + | ''Chlamydomonas reinhardtii'' | |
| − | + | ||
| − | + | ||
===References=== | ===References=== | ||
| + | Sirijovski, N., Lunqvist, J., Rosenback, M., Elmlund, H., Al-Karadaghi, S., Willows, R.D., Hansson, M. (2008). Substrate-binding Model of the Chlorophyll Biosynthetic Magnesium Chelatase BchH Subunit. Journal of Biological Chemistry, 283, 11652-11660. | ||
Latest revision as of 02:23, 19 September 2015
ChlH
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 856
Illegal BglII site found at 1606
Illegal BglII site found at 2229
Illegal BglII site found at 2308
Illegal BglII site found at 3615 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 1150
Illegal AgeI site found at 35
Illegal AgeI site found at 65
Illegal AgeI site found at 959
Illegal AgeI site found at 1127
Illegal AgeI site found at 2645
Illegal AgeI site found at 2699
Illegal AgeI site found at 2918 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 3044
Illegal SapI.rc site found at 401
Illegal SapI.rc site found at 2974
Design Notes
This part is to be combined with GUN4 to form operon-1, one of four operons engineered for synthesis of chlorophyll-biosynthesis pathway.
Magnesium chelatase sits at the branch point of the common tetrapyrrole pathway and inserts Mg2+ into Proto to produce Mg-Proto, the first unique intermediate of the chlorophyll biosynthetic pathway. It is known that the BchH/ChlH subunit binds the substrate and, for this reason, is thought to be the catalytic component of the enzyme. The ChlH subunit makes conformational changes upon binding its porphyrin substrate.
A study done on Rhodobacter capsulatus has demonstrated the apo structure to contain three major lobe-shaped domains connected at a single point, with additional densities at the tip of two lobes termed the “thumb” and “finger” (figure: 2). This independent reconstruction of a substrate-bound ChlH complex permitted insight into substrate-induced conformational changes (Sirijovski et al., 2008).
Source
Chlamydomonas reinhardtii
References
Sirijovski, N., Lunqvist, J., Rosenback, M., Elmlund, H., Al-Karadaghi, S., Willows, R.D., Hansson, M. (2008). Substrate-binding Model of the Chlorophyll Biosynthetic Magnesium Chelatase BchH Subunit. Journal of Biological Chemistry, 283, 11652-11660.