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1l5t
From Proteopedia
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| - | [[Image:1l5t.jpg|left|200px]] | + | [[Image:1l5t.jpg|left|200px]] |
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| - | '''Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form.''' | + | {{Structure |
| + | |PDB= 1l5t |SIZE=350|CAPTION= <scene name='initialview01'>1l5t</scene>, resolution 3.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Diferric-transferrin_reductase Diferric-transferrin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.1.2 1.16.1.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L5T is a [ | + | 1L5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5T OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form., Jameson GB, Anderson BF, Breyer WA, Day CL, Tweedie JW, Baker EN, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):955-62. Epub, 2002 May 29. PMID:[http:// | + | Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form., Jameson GB, Anderson BF, Breyer WA, Day CL, Tweedie JW, Baker EN, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):955-62. Epub, 2002 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12037297 12037297] |
[[Category: Diferric-transferrin reductase]] | [[Category: Diferric-transferrin reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: twinning]] | [[Category: twinning]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:46 2008'' |
Revision as of 10:26, 20 March 2008
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| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Diferric-transferrin reductase, with EC number 1.16.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form.
Contents |
Overview
Human lactoferrin is an iron-binding protein with a bilobal structure. Each lobe contains a high-affinity binding site for a single Fe(3+) ion and an associated CO(3)(2-) ion. Although iron binds very tightly, it can be released at low pH, with an accompanying conformational change in which the two domains move apart. The Arg121Asp (R121D) mutant of the N-lobe half-molecule of human lactoferrin was constructed in order to test whether the Asp121 side chain could substitute for the CO(3)(2-) ion at the iron-binding site. The R121D mutant protein was crystallized in its apo form as it lost iron during crystallization. The crystals were also merohedrally twinned, with a twin fraction close to 0.5. Starting from the initial molecular-replacement solution [Breyer et al. (1999), Acta Cryst. D55, 129-138], the structure has been refined at 3.0 A resolution to an R factor of 13.9% (R(free) of 19.9%). Despite the moderate resolution, the high solvent content and non-crystallographic symmetry contributed to electron-density maps of excellent quality. Weakened iron binding by the R121D mutant is explained by occlusion of the anion-binding site by the Asp side chain. The opening of the two domains in the apoR121D structure (a rotation of 54 degrees ) closely matches that of the N-lobe in full-length lactoferrin, showing that the extent of the conformational change depends on properties inherent to the N-lobe. Differences in the C-terminal portion of the N-lobe (residues 321-332) for apoR121D relative to the closed wild-type iron-bound structure point to the importance of this region in stabilizing the open form.
Disease
Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[602121]
About this Structure
1L5T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form., Jameson GB, Anderson BF, Breyer WA, Day CL, Tweedie JW, Baker EN, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):955-62. Epub, 2002 May 29. PMID:12037297
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