Difference between revisions of "Part:BBa K1640019:Design"

 
(Design Notes)
 
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<partinfo>BBa_K1640019 short</partinfo>
 
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===Design Notes===
 
===Design Notes===
n/a
 
  
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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.
  
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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===
 
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''Chlamydomonas reinhardtii''
n/a
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===References===
 
===References===
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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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE 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
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE 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
  • 1000
    INCOMPATIBLE 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.