1dly: Difference between revisions

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[[Image:1dly.gif|left|200px]]<br />

[[Image:1dly.gif|left|200px]]<br /><applet load="1dly" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1dly" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1dly, resolution 1.8Å" />

'''X-RAY CRYSTAL STRUCTURE OF HEMOGLOBIN FROM THE GREEN UNICELLULAR ALGA CHLAMYDOMONAS EUGAMETOS'''<br />

==Overview==

Small hemoproteins displaying amino acid sequences 20-40 residues shorter, than (non-)vertebrate hemoglobins (Hbs) have recently been identified in, several pathogenic and non-pathogenic unicellular organisms, and named, 'truncated hemoglobins' (trHbs). They have been proposed to be involved, not only in oxygen transport but also in other biological functions, such, as protection against reactive nitrogen species, photosynthesis or to act, as terminal oxidases. Crystal structures of trHbs from the ciliated, protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas, eugametos show that the tertiary structure of both proteins is based on a, 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing, of the classical 'three-over-three' alpha-helical globin fold. Based on, specific Gly-Gly motifs the tertiary structure accommodates the deletion, of the N-terminal A-helix and replacement of the crucial heme-binding, F-helix with an extended polypeptide loop. Additionally, concerted, structural modifications allow burying of the heme group and define the, distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural, and amino acid sequence consensus rules for stabilizing the fold and the, bound heme in the trHbs homology subfamily is deduced.

Small hemoproteins displaying amino acid sequences 20-40 residues shorter than (non-)vertebrate hemoglobins (Hbs) have recently been identified in several pathogenic and non-pathogenic unicellular organisms, and named 'truncated hemoglobins' (trHbs). They have been proposed to be involved not only in oxygen transport but also in other biological functions, such as protection against reactive nitrogen species, photosynthesis or to act as terminal oxidases. Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing of the classical 'three-over-three' alpha-helical globin fold. Based on specific Gly-Gly motifs the tertiary structure accommodates the deletion of the N-terminal A-helix and replacement of the crucial heme-binding F-helix with an extended polypeptide loop. Additionally, concerted structural modifications allow burying of the heme group and define the distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural and amino acid sequence consensus rules for stabilizing the fold and the bound heme in the trHbs homology subfamily is deduced.

==About this Structure==

1DLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_eugametos Chlamydomonas eugametos] with CYN, SO4, HEM and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DLY OCA].

1DLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_eugametos Chlamydomonas eugametos] with <scene name='pdbligand=CYN:'>CYN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLY OCA].

==Reference==

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[[Category: globin fold truncated hemoglobin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on Thu ~~Nov 8 13~~:00:~~07 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:06 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dly.gif|left|200px]]<br />
+[[Image:1dly.gif|left|200px]]<br /><applet load="1dly" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1dly" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1dly, resolution 1.8&Aring;" />
 '''X-RAY CRYSTAL STRUCTURE OF HEMOGLOBIN FROM THE GREEN UNICELLULAR ALGA CHLAMYDOMONAS EUGAMETOS'''<br />
 ==Overview==
-Small hemoproteins displaying amino acid sequences 20-40 residues shorter, than (non-)vertebrate hemoglobins (Hbs) have recently been identified in, several pathogenic and non-pathogenic unicellular organisms, and named, 'truncated hemoglobins' (trHbs). They have been proposed to be involved, not only in oxygen transport but also in other biological functions, such, as protection against reactive nitrogen species, photosynthesis or to act, as terminal oxidases. Crystal structures of trHbs from the ciliated, protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas, eugametos show that the tertiary structure of both proteins is based on a, 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing, of the classical 'three-over-three' alpha-helical globin fold. Based on, specific Gly-Gly motifs the tertiary structure accommodates the deletion, of the N-terminal A-helix and replacement of the crucial heme-binding, F-helix with an extended polypeptide loop. Additionally, concerted, structural modifications allow burying of the heme group and define the, distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural, and amino acid sequence consensus rules for stabilizing the fold and the, bound heme in the trHbs homology subfamily is deduced.
+Small hemoproteins displaying amino acid sequences 20-40 residues shorter than (non-)vertebrate hemoglobins (Hbs) have recently been identified in several pathogenic and non-pathogenic unicellular organisms, and named 'truncated hemoglobins' (trHbs). They have been proposed to be involved not only in oxygen transport but also in other biological functions, such as protection against reactive nitrogen species, photosynthesis or to act as terminal oxidases. Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing of the classical 'three-over-three' alpha-helical globin fold. Based on specific Gly-Gly motifs the tertiary structure accommodates the deletion of the N-terminal A-helix and replacement of the crucial heme-binding F-helix with an extended polypeptide loop. Additionally, concerted structural modifications allow burying of the heme group and define the distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural and amino acid sequence consensus rules for stabilizing the fold and the bound heme in the trHbs homology subfamily is deduced.
 ==About this Structure==
-DLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_eugametos Chlamydomonas eugametos] with CYN, SO4, HEM and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLY OCA].
+DLY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_eugametos Chlamydomonas eugametos] with <scene name='pdbligand=CYN:'>CYN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLY OCA].
 ==Reference==
@@ Line 26: / Line 25: @@
 [[Category: globin fold truncated hemoglobin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:00:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:06 2008''