2ex2: Difference between revisions
New page: left|200px<br /><applet load="2ex2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ex2, resolution 1.55Å" /> '''Crystal structure of... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2ex2.gif|left|200px]]<br /><applet load="2ex2" size=" | [[Image:2ex2.gif|left|200px]]<br /><applet load="2ex2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ex2, resolution 1.55Å" /> | caption="2ex2, resolution 1.55Å" /> | ||
'''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli'''<br /> | '''Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of penicillin binding protein 4 (PBP4) from | The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in the synthesis and maintenance of the cell wall. The model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds. The structures of the protein covalently attached to five different antibiotics presented here show the active site residues are unmoved compared to the apoprotein, but nearby surface loops and helices are displaced in some cases. The altered geometry of conserved active site residues compared with those of other PBPs suggests a possible cause for the slow deacylation rate of PBP4. | ||
==About this Structure== | ==About this Structure== | ||
2EX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2EX2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX2 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Kishida, H.]] | [[Category: Kishida, H.]] | ||
[[Category: Lloyd, A.]] | [[Category: Lloyd, A.]] | ||
[[Category: Park, S | [[Category: Park, S Y.]] | ||
[[Category: Roper, D | [[Category: Roper, D I.]] | ||
[[Category: Tame, J | [[Category: Tame, J R.H.]] | ||
[[Category: Unzai, S.]] | [[Category: Unzai, S.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
| Line 27: | Line 27: | ||
[[Category: penicillin-binding protein]] | [[Category: penicillin-binding protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:25 2008'' | ||
Revision as of 18:15, 21 February 2008
|
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli
OverviewOverview
The crystal structure of penicillin binding protein 4 (PBP4) from Escherichia coli, which has both DD-endopeptidase and DD-carboxypeptidase activity, is presented. PBP4 is one of 12 penicillin binding proteins in E. coli involved in the synthesis and maintenance of the cell wall. The model contains a penicillin binding domain similar to known structures, but includes a large insertion which folds into domains with unique folds. The structures of the protein covalently attached to five different antibiotics presented here show the active site residues are unmoved compared to the apoprotein, but nearby surface loops and helices are displaced in some cases. The altered geometry of conserved active site residues compared with those of other PBPs suggests a possible cause for the slow deacylation rate of PBP4.
About this StructureAbout this Structure
2EX2 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics., Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR, Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754
Page seeded by OCA on Thu Feb 21 17:15:25 2008