1kr5: Difference between revisions

Line 1:

[[Image:1kr5.gif|left|200px]]<br />

[[Image:1kr5.gif|left|200px]]<br /><applet load="1kr5" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1kr5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1kr5, resolution 2.10Å" />

'''Crystal structure of human L-isoaspartyl methyltransferase'''<br />

~~==Overview==~~

The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged, proteins by recognizing and methylating isomerized and racemized aspartyl, residues in aging proteins. The crystal structure of the human enzyme, containing a bound S-adenosyl-l-homocysteine cofactor is reported here at, a resolution of 2.1 A. A comparison of the human enzyme to homologs from, two other species reveals several significant differences among otherwise, similar structures. In all three structures, we find that three conserved, charged residues are buried in the protein interior near the active site., Electrostatics calculations suggest that these buried charges might make, significant contributions to the energetics of binding the charged, S-adenosyl-l-methionine cofactor and to catalysis. We suggest a possible, structural explanation for the observed differences in reactivity toward, the structurally similar l-isoaspartyl and d-aspartyl residues in the, human, archael, and eubacterial enzymes. Finally, the human structure, reveals that the known genetic polymorphism at residue 119 (Val/Ile) maps, to an exposed region away from the active site.

==About this Structure==

1KR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KR5 OCA].

1KR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR5 OCA].

~~==Reference==~~

Crystal structure of human L-isoaspartyl methyltransferase., Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO, J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11792715 11792715]

[[Category: Homo sapiens]]

[[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]]

[[Category: Single protein]]

[[Category: Clarke, S.]]

[[Category: Griffith, S.C.]]

[[Category: Griffith, S C.]]

[[Category: MacLaren, D.C.]]

[[Category: MacLaren, D C.]]

[[Category: Ryttersgaard, C.]]

[[Category: Sawaya, M.R.]]

[[Category: Sawaya, M R.]]

[[Category: Yeates, T.O.]]

[[Category: Yeates, T O.]]

[[Category: SAH]]

[[Category: rossmann-fold doubly-wound-alpha-beta-alpha-sandwich]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:53:~~52 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:03 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1kr5.gif|left|200px]]<br />
+[[Image:1kr5.gif|left|200px]]<br /><applet load="1kr5" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1kr5" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1kr5, resolution 2.10&Aring;" />
 '''Crystal structure of human L-isoaspartyl methyltransferase'''<br />
-==Overview==
-The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged, proteins by recognizing and methylating isomerized and racemized aspartyl, residues in aging proteins. The crystal structure of the human enzyme, containing a bound S-adenosyl-l-homocysteine cofactor is reported here at, a resolution of 2.1 A. A comparison of the human enzyme to homologs from, two other species reveals several significant differences among otherwise, similar structures. In all three structures, we find that three conserved, charged residues are buried in the protein interior near the active site., Electrostatics calculations suggest that these buried charges might make, significant contributions to the energetics of binding the charged, S-adenosyl-l-methionine cofactor and to catalysis. We suggest a possible, structural explanation for the observed differences in reactivity toward, the structurally similar l-isoaspartyl and d-aspartyl residues in the, human, archael, and eubacterial enzymes. Finally, the human structure, reveals that the known genetic polymorphism at residue 119 (Val/Ile) maps, to an exposed region away from the active site.
 ==About this Structure==
-KR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KR5 OCA].
+KR5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KR5 OCA].
-==Reference==
-Crystal structure of human L-isoaspartyl methyltransferase., Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO, J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11792715 11792715]
 [[Category: Homo sapiens]]
 [[Category: Protein-L-isoaspartate(D-aspartate) O-methyltransferase]]
 [[Category: Single protein]]
 [[Category: Clarke, S.]]
-[[Category: Griffith, S.C.]]
+[[Category: Griffith, S C.]]
-[[Category: MacLaren, D.C.]]
+[[Category: MacLaren, D C.]]
 [[Category: Ryttersgaard, C.]]
-[[Category: Sawaya, M.R.]]
+[[Category: Sawaya, M R.]]
-[[Category: Yeates, T.O.]]
+[[Category: Yeates, T O.]]
 [[Category: SAH]]
 [[Category: rossmann-fold doubly-wound-alpha-beta-alpha-sandwich]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:53:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:03 2008''