2c4c

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[[Image:2c4c.jpg|left|200px]]<br /><applet load="2c4c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c4c.jpg|left|200px]]
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caption="2c4c, resolution 2.90&Aring;" />
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'''CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL'''<br />
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{{Structure
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|PDB= 2c4c |SIZE=350|CAPTION= <scene name='initialview01'>2c4c</scene>, resolution 2.90&Aring;
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C4C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4C OCA].
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2C4C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4C OCA].
==Reference==
==Reference==
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High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule., Siebold C, Berrow N, Walter TS, Harlos K, Owens RJ, Stuart DI, Terman JR, Kolodkin AL, Pasterkamp RJ, Jones EY, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16836-41. Epub 2005 Nov 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16275925 16275925]
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High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule., Siebold C, Berrow N, Walter TS, Harlos K, Owens RJ, Stuart DI, Terman JR, Kolodkin AL, Pasterkamp RJ, Jones EY, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16836-41. Epub 2005 Nov 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16275925 16275925]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:10:39 2008''

Revision as of 14:10, 20 March 2008

Image:2c4c.jpg


PDB ID 2c4c

Drag the structure with the mouse to rotate
, resolution 2.90Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL


Overview

Semaphorins are extracellular cell guidance cues that govern cytoskeletal dynamics during neuronal and vascular development. MICAL (molecule interacting with CasL) is a multidomain cytosolic protein with a putative flavoprotein monooxygenase (MO) region required for semaphorin-plexin repulsive axon guidance. Here, we report the 1.45-A resolution crystal structure of the FAD-containing MO domain of mouse MICAL-1 (residues 1-489). The topology most closely resembles that of the NADPH-dependent flavoenzyme p-hydroxybenzoate hydroxylase (PHBH). Comparison of structures before and after reaction with NADPH reveals that, as in PHBH, the flavin ring can switch between two discrete positions. In contrast with other MOs, this conformational switch is coupled with the opening of a channel to the active site, suggestive of a protein substrate. In support of this hypothesis, distinctive structural features highlight putative protein-binding sites in suitable proximity to the active site entrance. The unusual juxtaposition of this N-terminal MO (hydroxylase) activity with the characteristics of a multiprotein-binding scaffold exhibited by the C-terminal portion of the MICALs represents a unique combination of functionality to mediate signaling.

About this Structure

2C4C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule., Siebold C, Berrow N, Walter TS, Harlos K, Owens RJ, Stuart DI, Terman JR, Kolodkin AL, Pasterkamp RJ, Jones EY, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16836-41. Epub 2005 Nov 7. PMID:16275925

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